{"title":"Growth Hormone","description":"","products":[{"product_id":"ipamorelin","title":"Ipamorelin","description":"\u003cp dir=\"ltr\"\u003eIpamorelin is a synthetic peptide that is composed of five amino acids, otherwise known as a pentadecapeptide (Aib-His-D-2-Nal-D-Phe-Lys-NH2), formally classified as a Growth Hormone Secretagogue (GHS). Its name is derived from the intention of its development. Ipamorelin peptide was designed to act via ghrelin receptor binding. The ghrelin receptors on the pituitary gland (the gland naturally involved with growth hormone, or hGH synthesis) are also known as Growth Hormone Secretagogue receptors (GHS-R). Through its implied action, Ipamorelin may host the potential to trigger the GHS-Rs on the pituitary gland and potentially stimulate the release of growth hormone.\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eIpamorelin is the first synthetic GHS that appears highly selective and may have the potential to augment the production of hGH without affecting other pituitary hormones such as prolactin or adrenocorticotropic hormone (ACTH). The potential increase in hGH might promote lipolysis and insulin-like growth factor-1 (IGF-1) production synthesis. Consequently, IGF-1 may become a mediator of hGH’s anabolic actions, and thereby the peptide may act to increase cellular proliferation and bone and muscle anabolism.\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003eChemical Makeup\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Formula:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003eC\u003csub dir=\"ltr\"\u003e38\u003c\/sub\u003eH\u003csub dir=\"ltr\"\u003e49\u003c\/sub\u003eN\u003csub dir=\"ltr\"\u003e9\u003c\/sub\u003eO\u003csub dir=\"ltr\"\u003e5\u003c\/sub\u003e\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Weight:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003e711.86 g\/mol\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eOther Known Titles:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003eNNC 26-0161\u003c\/p\u003e\n\u003ch2\u003eResearch and Clinical Studies\u003c\/h2\u003e\n\u003ch3\u003e\u003cem\u003eIpamorelin Peptide and Selective Agonism\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eBased on one 1998 murine model-based research study, researchers suggested that Ipamorelin may release growth hormones from the pituitary cells. When Ipamorelin was presented to swine and pentobarbitone anesthetized rats, it reportedly exhibited release in growth hormones. Upon further observation, the researchers hypothesized that similar to other growth hormone (GH) stimulating peptides, Ipamorelin may be a growth receptor agonist stimulating GH release through potential affinity in growth hormone receptors. Moreover, the researchers commented that Ipamorelin appears to be the first GHS-R “\u003cem dir=\"ltr\"\u003eagonist with a selectivity for GH release similar to that displayed by GHRH. The specificity of Ipamorelin makes this compound a very interesting candidate for future clinical development.\u003c\/em\u003e”\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eScientific research studies have also suggested that Ipamorelin may lead to increased hGH secretion, possibly without significantly affecting other pituitary hormones such as the levels of prolactin or ACTH.\u003csup dir=\"ltr\"\u003e(2)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eIpamorelin Peptide and Growth Hormone Synthesis\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eStudies conducted\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003ein vitro\u003cspan\u003e \u003c\/span\u003e\u003c\/em\u003esuggest that the interaction of Ipamorelin with GHS receptors may potentially affect somatotroph cells in the anterior pituitary gland by triggering a series of cellular signaling events.\u003csup dir=\"ltr\"\u003e(3)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThis theorized pathway involves the activation of phospholipase C (PLC), which some researchers believe may lead to the increased release of inositol triphosphate (IP3) and diacylglycerol (DAG). This release of secondary messenger molecules such as IP3 might potentially stimulate the discharge of calcium ions (Ca2+) from the cell's internal stores, while DAG might activate protein kinase C (PKC). The subsequent rise in intracellular calcium levels and the possible activation of PKC are thought to result in the exocytosis of vesicles filled with growth hormones from these pituitary cells.\u003csup dir=\"ltr\"\u003e(3)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eIn late 1999, a clinical trial was carried out on eight test subjects where Ipamorelin was presented every 15 minutes for a set period. Two hours post-study, it was suggested by the researchers that the levels of growth hormone had apparently increased. More specifically, Ipamorelin appeared to have tended to boost growth hormone levels, potentially soaring to as much as 80mIU\/l (roughly equivalent to a concentration of about 26.6ng\/ml). When this increase is measured as a percentage compared to a placebo (with a baseline of 1.31mIU\/l or 0.4ng\/ml), the enhancement appeared to have exceeded a 60-fold uplift.\u003csup dir=\"ltr\"\u003e(4)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eIpamorelin Peptide and Bone Tissue\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eIt is conceivable that Ipamorelin may positively influence bone mineral density. The theory posits that Ipamorelin might stimulate osteoblasts (cells responsible for bone formation) via hGH-mediated mechanisms, potentially leading to their enhanced proliferation, growth, and specialization. In a particular study, murine models were exposed to either Ipamorelin or a placebo.\u003csup dir=\"ltr\"\u003e(5)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThe impact of Ipamorelin on bone mineral density in these mice was monitored closely through real-time dual X-ray absorptiometry (DEXA) assessments at critical sites, including the femur and L6 vertebra. Post-experiment, the femur bones were further examined using mid-diaphyseal peripheral quantitative computed tomography (pQCT) scans. Preliminary findings implied that the peptide may have contributed to increased body mass and a probable elevation in the overall tibial and vertebral BMC (bone mineral content) as detected by DEXA compared to the placebo group. Further, the pQCT data appeared to suggest that the observed augmentation in cortical BMC may have stemmed from an enlargement in the cross-sectional area of the bone. In contrast, the cortical volumetric bone mineral density (BMD, which denotes the ratio of BMC to area) appeared to remain steady. Thus, there may have been an enlargement in the volumes of the femur and the L6 vertebrae since BMC appeared to increase while the volumetric BMDs appeared unchanged.\u003csup dir=\"ltr\"\u003e(5)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eIpamorelin Peptide and Digestion\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eResearchers have delved into the potential of Ipamorelin in the functionality of the stomach, with a keen interest in its ability to possibly expedite the process of gastric emptying. For example, one study employed a technique to ascertain gastric emptying rates, which entailed monitoring the proportion of a marked substance that lingered in the stomach 15 minutes after its introduction through intragastric gavage.\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThe scientists conducted surgeries to purposefully decelerate the gastric emptying process in murine models. This deceleration was particularly noticeable in the control group. In contrast, Ipamorelin appeared to have markedly accelerated the emptying process compared to the control. This observation led the team to hypothesize that Ipamorelin might be able to increase the velocity of gastric emptying. Additional research was initiated to delve deeper into the action of the compound on the contractile potential of the stomach's smooth muscles, which were activated by acetylcholine and electrical field stimulation. Indeed, the decelerated peristalsis appeared to be mitigated when Ipamorelin and ghrelin were studied together, suggesting the idea that Ipamorelin may enhance the contractility of gastric smooth muscles.\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eIpamorelin Peptide and Appetite\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eThe potential actions of Ipamorelin on ghrelin receptors may lead to an enhancement in hunger signals and, perhaps, an ensuing augmentation in body mass. Research suggests that research models exposed to Ipamorelin were observed to sustain an estimated 15% surge in body weight.\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eResearchers speculate that this substance might have led to a proportional increase in the weight of fat pads in comparison to the total body weight. Consequently, DEXA scans might indicate a comparative rise in body fat percentage. Moreover, there is speculation among researchers that Ipamorelin might elevate serum leptin levels, a hormone considered to play a crucial role in energy balance and hunger regulation. This observation has prompted scientists to consider increased food consumption as a potential contributor to the weight gain noted in research models exposed to Ipamorelin. They have posited that \"\u003cem dir=\"ltr\"\u003eGHSs increase body fat by GH-independent mechanisms that may include increased feeding.\u003c\/em\u003e”\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eIpamorelin Peptide and Nitrogen Balance\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eResearchers have suggested that Ipamorelin may potentially mediate anabolic action, which may be due to its potential in hGH and IGF-1 synthesis and may be assessed through its impact on nitrogen balance. In a distinct investigation, researchers aimed to explore the action of Ipamorelin on specific liver markers associated with alpha-amino-nitrogen conversion during induced catabolic states.\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThe study focused on the liver’s capacity to synthesize urea-N (CUNS), which may serve as an indicator of the organ's ability to process nitrogen. The levels of messenger RNA (mRNA) related to liver urea cycle enzymes were scrutinized, alongside an assessment of the overall nitrogen balance and a hypothesis regarding nitrogen distribution across various organs. The findings suggested that Ipamorelin might have contributed to a possible 20% reduction in CUNS compared to the artificially induced catabolic condition. Furthermore, it might have diminished the expression of urea cycle enzymes, possibly restored nitrogen balance, and, in theory, altered or improved nitrogen concentrations in different organs.\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong dir=\"ltr\"\u003eIpamorelin peptide is available for research and laboratory purposes only.\u003c\/strong\u003e\u003c\/em\u003e\u003c\/p\u003e\n\u003ch3\u003eReferences:\u003c\/h3\u003e\n\u003col\u003e\n\u003cli\u003eK. Raun et al., Ipamorelin, the first selective growth hormone secretagogue, Endocrinology, November 1998.\u003c\/li\u003e\n\u003cli\u003eSinha DK, Balasubramanian A, Tatem AJ, Rivera-Mirabal J, Yu J, Kovac J, Pastuszak AW, Lipshultz LI. Beyond the androgen receptor: the role of growth hormone secretagogues in the modern management of body composition in hypogonadal males. Transl Androl Urol. 2020 Mar;9(Suppl 2):S149-S159. doi: 10.21037\/tau.2019.11.30. PMID: 32257855; PMCID: PMC7108996\u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7108996\/\" rel=\"noopener\" dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7108996\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eJiménez-Reina, L., Cañete, R., de la Torre, M. J., \u0026amp; Bernal, G. (2002). Influence of chronic treatment with the growth hormone secretagogue Ipamorelin, in young female rats: somatotroph response in vitro. Histology and histopathology, 17(3), 707–714.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.14670\/HH-17.707\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.14670\/HH-17.707\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eGobburu, J.V.S., Agersø, H., Jusko, W.J. et al. Pharmacokinetic-Pharmacodynamic Modeling of Ipamorelin, a Growth Hormone Releasing Peptide, in Human Volunteers. Pharm Res 16, 1412–1416 (1999).\u003c\/li\u003e\n\u003cli\u003eSvensson, J., Lall, S., Dickson, S. L., Bengtsson, B. A., Rømer, J., Ahnfelt-Rønne, I., Ohlsson, C., \u0026amp; Jansson, J. O. (2000). The GH secretagogues ipamorelin and GH-releasing peptide-6 increase bone mineral content in adult female rats.\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eThe Journal of endocrinology\u003c\/em\u003e,\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003e165\u003c\/em\u003e(3), 569–577.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1677\/joe.0.1650569\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1677\/joe.0.1650569\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eGreenwood-Van Meerveld, B., Tyler, K., Mohammadi, E., \u0026amp; Pietra, C. (2012). Efficacy of ipamorelin, a ghrelin mimetic, on gastric dysmotility in a rodent model of postoperative ileus. Journal of experimental pharmacology, 4, 149–155.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.2147\/JEP.S35396\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.2147\/JEP.S35396\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eLall, S., Tung, L. Y., Ohlsson, C., Jansson, J. O., \u0026amp; Dickson, S. L. (2001). Growth hormone (GH)-independent stimulation of adiposity by GH secretagogues. Biochemical and biophysical research communications, 280(1), 132–138.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1006\/bbrc.2000.4065\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1006\/bbrc.2000.4065\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eAagaard, N. K., Grøfte, T., Greisen, J., Malmlöf, K., Johansen, P. B., Grønbaek, H., Ørskov, H., Tygstrup, N., \u0026amp; Vilstrup, H. (2009). Growth hormone and growth hormone secretagogue effects on nitrogen balance and urea synthesis in steroid treated rats.\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eGrowth hormone \u0026amp; IGF research: official journal of the Growth Hormone Research Society and the International IGF Research Society\u003c\/em\u003e,\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003e19\u003c\/em\u003e(5), 426–431.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1016\/j.ghir.2009.01.001\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1016\/j.ghir.2009.01.001\u003c\/a\u003e\n\u003c\/li\u003e\n\u003c\/ol\u003e","brand":"PureX Labs","offers":[{"title":"5mg","offer_id":48098749939956,"sku":null,"price":30.0,"currency_code":"USD","in_stock":true},{"title":"10mg","offer_id":47487371313396,"sku":null,"price":50.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0804\/5802\/3156\/files\/Ipamorelin.png?v=1769106217"},{"product_id":"igf-1-lr3","title":"IGF-1 LR3","description":"\u003cp dir=\"ltr\"\u003eInsulin-like Growth factor-1, or IGF-1, is a naturally produced protein with 70 amino acids. Receptor Grade IGF-1 LR3 is a synthetic variant of the naturally occurring IGF-1, which contains an extended N-terminal structure of 13 amino acids and a replacement of the glutamic acid at residue 3 with arginine. Hence, it is named IGF-1 Long R3.\u003csup dir=\"ltr\"\u003e(1)(2)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eOwing to the altered structure, Receptor Grade IGF-1 LR3 has been suggested to have increased affinity and increased anabolic potential while also binding less to IGF-1 binding proteins (IGF-1BPs). Structurally similar to insulin, this IGF-1 LR3 has the potential primarily to regulate cell tissue growth and development. This potential has been evaluated in cell growth studies, throughout which researchers first prompted the need for developing this high-potency variant. Moreover, the classification of\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eReceptor Grade\u003c\/em\u003e\u003cspan\u003e \u003c\/span\u003erefers to the purity of the material, which is considered higher than Media Grade IGF-1 LR3.\u003c\/p\u003e\n\u003ch3 dir=\"ltr\"\u003eChemical Makeup\u003csup dir=\"ltr\"\u003e(2,3)\u003c\/sup\u003e\n\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Formula:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003eC\u003csub dir=\"ltr\"\u003e400\u003c\/sub\u003eH\u003csub dir=\"ltr\"\u003e625\u003c\/sub\u003eN\u003csub dir=\"ltr\"\u003e111\u003c\/sub\u003eO\u003csub dir=\"ltr\"\u003e115\u003c\/sub\u003eS\u003csub dir=\"ltr\"\u003e9\u003c\/sub\u003e\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Weight:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003e9117.5 g\/mol\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eOther Known Titles:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003eLong-(arg3) insulin-like growth factor-I, Insulin-like growth factor long chain R3\u003c\/p\u003e\n\u003ch2\u003eResearch and Clinical Studies\u003c\/h2\u003e\n\u003ch3\u003e\u003cem\u003eReceptor Grade IGF-1 LR3 and Anabolic Potential\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eUnfortunately, research on the anabolic potential of IGF-1 LR3 is lacking, as the peptide is aimed towards cell culture studies. Yet, of the few experiments in murine models, researchers have suggested the significant potential of the peptide.\u003csup dir=\"ltr\"\u003e(1)\u003cspan\u003e \u003c\/span\u003e\u003c\/sup\u003eIn one study, experiments were carried out on normal and dexamethasone-induced catabolic murine models. It was noted that IGF-1 LR3 might potentially be 1.5 to 2 times as anabolic as IGF-I in inducing weight gain, increasing visceral organ weights, and possibly enhancing feed use efficiency under continuous delivery conditions. Moreover, IGF-1 LR3 appeared to have retained the potential for greater potency than IGF-I in several metrics, even in studies of only intermittent exposure. Additionally, in murine models exposed to dexamethasone, it was observed that the excretion of Nτ-methylhistidine—a marker indicative of muscle protein breakdown—appeared reduced to a greater extent by IGF-1 LR3, potentially threefold more than by IGF-I. This suggests that IGF-1 LR3 may host the potential, though not consistently equivalent across all parameters, to exhibit enhanced anabolic actions under certain laboratory conditions.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eTherefore, Receptor Grade IGF-1 LR3 may be posited to exert even greater anabolic potential than IGF-1. To provide a comparison, several studies have researched the anabolic potential of IGF-1. For example, a study\u003csup dir=\"ltr\"\u003e(4)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ewas conducted in 2005 to study the potential of the peptide in models of IGF-1 deficiency. Following peptide exposure, the length and growth of the models were assessed and analyzed against control thresholds. Based on the study findings, it was observed that total length increased in all peptide-exposed models by a significant margin against the control standards. This study suggests that IGF-1, and possibly also more potent analogs like Receptor Grade IGF-1 LR3 peptide, may have some potential in mitigating growth deficiency.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eReceptor Grade IGF-1 LR3 and Insulin Receptor Sensitivity\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eResearch\u003csup dir=\"ltr\"\u003e(5)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ehas suggested that IGF proteins typically bind to IGF-1 receptors and may stimulate glucose uptake, potentially through a signaling mechanism involving PI3K and AMPK pathways. However, when studied, peptides like Receptor Grade IGF-1 LR3 appeared to induce glucose uptake not just through IGF-1 receptor interactions but also independently, possibly via other pathways or receptors. This suggests that the mechanism of glucose uptake might involve additional cellular processes beyond the traditional receptor binding. Assefa B Mahmoud\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eet al. stated, \"Multiple [...] studies reported the role of IGF-1 in enhancing insulin sensitivity and glucose metabolism. A low-serum level of IGF-1 has been associated with insulin resistance, and [...] recombinant IGF-1 has been [hypothesized] to improve insulin sensitivity and glucose metabolism.”\u003c\/em\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eReceptor Grade IGF-1 LR3 and Cell Lifespan\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eResearch\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eon murine models observed that common markers of physiological decline, such as muscle tears and neurological deficiencies, appeared to be mitigated for an extended period following routine exposure to the peptide. While more detailed studies and clinical trials are pending, the above preliminary study suggests that the peptide may indirectly help to increase lifespan of functional cells. As per William E. Sonntag\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eet al.,\u003c\/em\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e“Based on this review, we conclude that the perceived contradictory roles of growth hormone and insulin-like growth factor-1 in the genesis of the aging phenotype should not be interpreted as a controversy on whether growth hormone or insulin-like growth factor-1 increases or decreases life span but rather as an opportunity to explore the complex roles of these hormones during specific stages of the life span.”\u003c\/em\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eReceptor Grade IGF-1 LR3 and Muscle Cells\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eA study\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ewas conducted on female murine models to identify the IGF-1 LR3 peptide’s potential in decreasing the action of myostatin. Myostatin is considered to prevent cellular differentiation; mitigating the actions of this protein may increase lean muscle and reduce fat cell storage and fatty mass. The study's results suggested that the various IGF-1 analogs, including Receptor Grade IGF-1 LR3, appear to potentially reverse adverse myostatin and prevent apoptosis.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eReceptor Grade IGF-1 LR3 and Shorter Action\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eAn experimental mouse model was created for a study\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ewhere the IGF-1 LR3 peptide was compared to the endogenous IGF-1. Throughout the study, it was observed that when the peptide was exposed to the murine model, it appeared to quickly clear from the serum and evenly distribute into tissue. More specifically, the researchers posited that IGF-1 LR3 cleared faster as it appeared to bind to a lower degree to binding proteins than endogenous IGF-1. This reduced binding affinity means IGF-1 LR3 might circulate more freely than IGF-I. The analysis of tissue distribution patterns of IGF-1 LR3 also suggested a potentially unique localization compared to IGF-I. Elevated levels of the IGF-1 LR3 tracer were observed in tissues such as kidneys, ovaries, and adrenal glands in murine models. This distinct distribution suggests that the organs primarily involved in metabolic and reproductive functions may exhibit varying capacities for the uptake or retention of IGF-1 LR3 in contrast to IGF-I. It is hypothesized that these differences might stem from IGF-1 LR3's diminished propensity to form complexes with IGFBPs, which might influence its bioavailability and interaction with target tissues in experimental models. Nevertheless, further research suggested that a peptide with similar modifications (namely R3) to IGF-1 LR3 may exert increased anabolic potential compared to regular IGF-1 despite the shorter action.\u003csup dir=\"ltr\"\u003e(9)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong dir=\"ltr\"\u003eReceptor Grade IGF-1 LR3 peptide is available for research and laboratory purposes only.\u003c\/strong\u003e\u003c\/em\u003e\u003c\/p\u003e\n\u003ch3\u003eReferences\u003c\/h3\u003e\n\u003col\u003e\n\u003cli\u003eTomas, F. M., Knowles, S. E., Owens, P. C., Chandler, C. S., Francis, G. L., Read, L. C., \u0026amp; Ballard, F. J. (1992). Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats. The Biochemical journal, 282 ( Pt 1)(Pt 1), 91–97.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC1130894\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC1130894\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eHuman Insulin-like growth factor. Protein Data Bank in Europe,\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ebi.ac.uk\/pdbe\/entry\/pdb\/1gzr\"\u003ehttps:\/\/www.ebi.ac.uk\/pdbe\/entry\/pdb\/1gzr\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eNational Center for Biotechnology Information (2023). PubChem Substance Record for SID 381123731, M9L22Y19H9, Source: ChemIDplus. Retrieved January 24, 2023 from\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubchem.ncbi.nlm.nih.gov\/substance\/381123731\"\u003ehttps:\/\/pubchem.ncbi.nlm.nih.gov\/substance\/381123731\u003c\/a\u003e.\u003c\/li\u003e\n\u003cli\u003eAnderson, L. J., Tamayose, J. M., \u0026amp; Garcia, J. M. (2018). Use of growth hormone, IGF-I, and insulin for anabolic purpose: Pharmacological basis, methods of detection, and adverse effects. Molecular and cellular endocrinology, 464, 65–74.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5723243\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5723243\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eAssefa, B., Mahmoud, A. M., Pfeiffer, A., Birkenfeld, A. L., Spranger, J., \u0026amp; Arafat, A. M. (2017). Insulin-Like Growth Factor (IGF) Binding Protein-2, Independently of IGF-1, Induces GLUT-4 Translocation and Glucose Uptake in 3T3-L1 Adipocytes. Oxidative medicine and cellular longevity, 2017\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5750484\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5750484\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eWilliam E. Sonntag, Anna Csiszar, Raphael de Cabo, Luigi Ferrucci, Zoltan Ungvari, Diverse Roles of Growth Hormone and Insulin-Like Growth Factor-1 in Mammalian Aging: Progress and Controversies, The Journals of Gerontology: Series A, Volume 67A, Issue 6, June 2012, Pages 587–598,\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1093\/gerona\/gls115\"\u003ehttps:\/\/doi.org\/10.1093\/gerona\/gls115\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eNaisi Li, Qiyuan Yang, Ryan G. Walker, Thomas B. Thompson, Min Du, Buel D. Rodgers, Myostatin Attenuation In Vivo Reduces Adiposity, but Activates Adipogenesis, Endocrinology, Volume 157, Issue 1, 1 January 2016, Pages 282–291.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1210\/en.2015-1546\"\u003ehttps:\/\/doi.org\/10.1210\/en.2015-1546\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eBastian SE, Walton PE, Wallace JC, Ballard FJ. Plasma clearance and tissue distribution of labelled insulin-like growth factor-I (IGF-I) and an analogue LR3IGF-I in pregnant rats. J Endocrinol. 1993 Aug;138(2):327-36.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1677\/joe.0.1380327\"\u003edoi: 10.1677\/joe.0.1380327\u003c\/a\u003e. PMID: 7693845.\u003c\/li\u003e\n\u003cli\u003eElis S, Wu Y, Courtland HW, Cannata D, Sun H, Beth-On M, Liu C, Jasper H, Domené H, Karabatas L, Guida C, Basta-Pljakic J, Cardoso L, Rosen CJ, Frystyk J, Yakar S. Unbound (bioavailable) IGF1 enhances somatic growth. Dis Model Mech. 2011 Sep;4(5):649-58.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1242\/dmm.006775\"\u003edoi: 10.1242\/dmm.006775\u003c\/a\u003e. Epub 2011 May 31. PMID: 21628395; PMCID: PMC3180229.\u003c\/li\u003e\n\u003c\/ol\u003e","brand":"PureX Labs","offers":[{"title":"0.1mg","offer_id":47487377146100,"sku":null,"price":25.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0804\/5802\/3156\/files\/IGF-1_LR3.png?v=1769106217"},{"product_id":"tesamorelin","title":"Tesamorelin","description":"\u003cp dir=\"ltr\"\u003eTesamorelin is a synthetic polypeptide composed of 44 amino acids analogous to growth hormone-releasing hormone. The N-terminus of the compound has been modified compared to growth hormone-releasing hormone, the modification of which researchers suggest may lead to improved stability.\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eTesamorelin has been studied for its potential mechanism of action, posited to be similar to growth hormone-releasing hormones (GHRH) receptors located at the anterior pituitary gland, possibly leading to increased production and secretion of growth hormones. Growth hormones may act on several cells, including hepatocytes, stimulating the systemic synthesis of insulin-like growth factor-1 (IGF-1). In addition, growth hormone may also stimulate IGF-1 production locally, inside various tissues.\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eIGF-1 has been posited to be the main anabolic mediator of growth hormone, potentially working to stimulate growth and inhibit programmed cell death.\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eOn the other hand, growth hormone itself is suggested to be lipolytic, inducing fat breakdown at specific adipose depots, such as abdominal and visceral fat depositions. Tesamorelin appears to stimulate the release of growth hormone, and consequently IGF-1, by potentially interacting with the GHRH receptors in the anterior pituitary gland cells. When Tesamorelin interacts with the GHRH receptor, it is hypothesized that this interaction might alter the receptor's structure, potentially initiating communication pathways within the cell. It is also theorized that Tesamorelin might enhance the production of cyclic adenosine monophosphate (cAMP) in certain cells. This process may occur through the stimulation of adenylate cyclase, an enzyme that converts adenosine triphosphate (ATP) into cAMP. Increased cAMP levels may lead to the activation of protein kinase A (PKA), an enzyme deemed critical for transmitting signals within cells. Activated PKA may phosphorylate various target proteins, triggering a cascade of cellular responses. The conjectural stimulation of the GHRH receptor by Tesamorelin and the cAMP-PKA signaling pathway might promote the secretion and distribution of growth hormone (hGH) from somatotroph cells in the pituitary gland. Research indicates that this peptide may lead to an estimated 69% increase in overall growth hormone levels, measured by the area under the curve (AUC), and a reported 55% increase in the mean pulse area of the growth hormone. However, it does not seem to influence the frequency or peak levels of growth hormone pulses. Additionally, IGF-1 levels apparently surged by 122%.\u003csup dir=\"ltr\"\u003e(3)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eThe N-terminus and C-terminus of the GHRH molecule are altered in Tesamorelin, potentially lending stability to the peptide and possibly increasing the compound's resistance to enzyme deactivation compared to natural GHRH.\u003csup dir=\"ltr\"\u003e(4)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eFocusing on the specific alterations, the C-terminus of Tesamorelin is modified by the addition of a trans-3-hexenoic acid group. This particular change, often referred to as an omega-amino acid modification, is believed to potentially reinforce the peptide's defense against enzymatic breakdown. On the other end, the N-terminus is modified by the attachment of an acetyl group, represented by the chemical notation CH₃CO-. This acetylation might enhance not only the molecule's stability but also its biological activity. As a result of these specific modifications, Tesamorelin is designated chemically as N-(trans-3-hexenoyl)-[Tyr1]hGRF(1–44)NH2 acetate, highlighting the specific alterations made to the peptide.\u003c\/p\u003e\n\u003ch3\u003eChemical Makeup\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Formula:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003eC\u003csub dir=\"ltr\"\u003e221\u003c\/sub\u003eH\u003csub dir=\"ltr\"\u003e366\u003c\/sub\u003eN\u003csub dir=\"ltr\"\u003e72\u003c\/sub\u003eO\u003csub dir=\"ltr\"\u003e67\u003c\/sub\u003eS\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Weight:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003e5136 g\/mol\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eOther Known Titles:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003e(3E)-hex-3-enoylsomatoliberin\u003c\/p\u003e\n\u003ch2\u003eResearch and Clinical Studies\u003c\/h2\u003e\n\u003ch3\u003e\u003cem\u003eTesamorelin Peptide and Lipodystrophy\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp\u003eLipodystrophy models refer to abnormal or pathological fat distribution and metabolism. The primary feature of lipodystrophy is the irregular distribution of fat into depots, leading to loss of fat (lipoatrophy) from specefic areas, and accumulation of excess fat (lipohypertrophy) in other regions. This abnormal fat distribution is often associated with serious negative metabolic changes, including insulin resistance, elevated cholesterol and triglyceride levels. Test models exhibiting lipodystrophy report low levels of GH and IGF-1. Researchers studying Tesamorelin's action and potential impact, suggest that the peptide may positively influence lipid metabolism, especially in lipodystrophy models.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eFor example, two phase III studies\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ewere conducted with 806 test subjects over 26 weeks, followed by another 26-week extension. Each of the 806 test subjects had immunodeficiencies and lipodystrophy. The subjects were divided into two groups; one group with 543 subjects was presented with Tesamorelin, and the remaining 263 subjects were presented with a placebo for 26 weeks. After this duration, the Tesamorelin subjects were again randomly divided into 2 groups, in which one group continued Tesamorelin influence, and the other half was presented with a placebo for another 26 weeks. At week 26, the researchers observed a significant decrease in visceral adipose tissue level amongst the Tesamorelin subjects, at least 15.4%. Additionally, the levels of triglyceride and cholesterol were reported significantly decreased compared to the placebo group.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eTesamorelin Peptide and Immunodeficient Fat Fractions\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eResearchers posit that serious immunodeficiencies may induce non-alcoholic fatty liver disease (NAFLD), which in clinical cases is reported in nearly 40% of HIV-positive test models.\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eIn this study,\u003csup dir=\"ltr\"\u003e(5)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003e61 test subjects with HIV and a high hepatic fat fraction (HFF) were selected as test models. These subjects were influenced with Tesamorelin or a placebo for 12 months. The rate of HFF was monitored at the end of the study. After 12 months, it was reported by the researchers that 35% of subjects presented with Tesamorelin exhibited an apparent reduction in HFF rate by less than 5% vs. only 4% of subjects receiving placebo exhibited any HFF reduction. There was no reported alteration in the glucose levels.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eTesamorelin Peptide and Cognition\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eIn this clinical study,\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eimmunodeficient models with mild cognitive impairment were observed. The main intent of this study was to determine Tesamorelin's potential effect on neurological functioning. 100 subjects, aged more than 40 years, participated in this trial and underwent Tesamorelin presentation daily for 6 months, followed by all absence of Tesamorelin influence for the next 6 months. Then Tesamorelin was re-introduced once a day for another 6 months. The primary outcome of this study was reported in changes in neurocognitive performance measured by the Global Deficit Score (GDS) after 6 and 12 months. This study is underway, and the final results have not been published.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eTesamorelin Peptide and Insulin\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eThe main aim of this study\u003csup dir=\"ltr\"\u003e(9)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ewas to determine any potential Tesamorelin might exhibit in altering insulin sensitivity. In this clinical trial setting, 53 test subjects with Type II diabetes were observed in this 12-week randomized trial. The subjects were divided into three groups, each receiving a lower or higher concentration of Tesamorelin or a placebo. Following the study period of 12 weeks, the concentration of fasting glucose, glycosylated hemoglobin, and diabetes control was measured. There was no reported significant reduction in either of these parameters. The results of all three groups appeared to be indifferent.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eTesamorelin Peptide and Muscle Tissue\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eIn a research investigation, the possible impacts of Tesamorelin on the structural quality of muscle tissues were evaluated using computed tomography (CT) scans.\u003csup dir=\"ltr\"\u003e(10)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eComputed tomography (CT) is an imaging tool that combines X-rays and computer technology to produce detailed pictures of internal structures. The findings from this study tentatively suggested a potential association between Tesamorelin and improvements in the density and overall volume of muscle tissues. It was observed that specific muscle groups, particularly the\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003erectus abdominis\u003c\/em\u003e,\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003epsoas major\u003c\/em\u003e, and\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eparaspinal muscles\u003c\/em\u003e, exhibited more noticeable variations. These variations consisted of either increased muscle density and volume or decreased fat within the muscle tissue. From a statistical perspective, the alterations in muscle density and size or the reduction in fat content in these specific muscles were significantly different when compared to results from a control group receiving a placebo.\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eTesamorelin Peptide and Visceral Fat\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eVisceral obesity involves the accumulation of excess fat around and within internal organs, a condition often observed in models of lipodystrophy—a disorder characterized by abnormal distribution of fat cells. This form of excessive fat accumulation is potentially linked to several metabolic issues. These issues include insulin resistance, a diminished ability to respond to insulin leading to elevated blood glucose levels. Additionally, visceral obesity is associated with the development of atherosclerosis, a condition where plaque builds up in the arteries, elevated levels of low-density lipoprotein (LDL) cholesterol, and hyperuricemia, an excess of uric acid. The significance of these models extends beyond aesthetic concerns, indicating that lipodystrophy may precipitate profound metabolic disturbances. In addressing these challenges, Tesamorelin, a synthetic form of the growth-hormone-releasing factor, has been proposed as a possibly positive avenue for further development. Research into Tesamorelin has suggested it may lead to a reduction of up to 25% in visceral fat among lipodystrophy models.\u003csup dir=\"ltr\"\u003e(11)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong dir=\"ltr\"\u003eTesamorelin peptide is available for research and laboratory purposes only. Please review and adhere to our\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" href=\"https:\/\/www.corepeptides.com\/terms\/\"\u003eTerms and Conditions\u003c\/a\u003e\u003cspan\u003e \u003c\/span\u003ebefore ordering.\u003c\/strong\u003e\u003c\/em\u003e\u003c\/p\u003e\n\u003ch3\u003eReferences:\u003c\/h3\u003e\n\u003col\u003e\n\u003cli\u003eClinical and Research Information on Drug-Induced Liver Injury [Internet]. Bethesda (MD): National Institute of Diabetes and Digestive and Kidney Diseases; 2012-. Tesamorelin. [Updated 2018 Oct 20].\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK548730\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/books\/NBK548730\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eSpooner, L. M., \u0026amp; Olin, J. L. (2012). Tesamorelin: a growth hormone-releasing factor analogue for HIV-associated lipodystrophy. The Annals of pharmacotherapy, 46(2), 240–247.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1345\/aph.1Q629\"\u003ehttps:\/\/doi.org\/10.1345\/aph.1Q629\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eStanley TL, Chen CY, Branch KL, Makimura H, Grinspoon SK. Effects of a growth hormone-releasing hormone analog on endogenous GH pulsatility and insulin sensitivity in healthy men. J Clin Endocrinol Metab. 2011 Jan;96(1):150-8. doi: 10.1210\/jc.2010-1587. Epub 2010 Oct 13. PMID: 20943777; PMCID: PMC3038486.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3038486\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3038486\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eFerdinandi ES, Brazeau P, High K, Procter B, Fennell S, Dubreuil P. Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue. Basic Clin Pharmacol Toxicol. 2007 Jan;100(1):49-58. doi: 10.1111\/j.1742-7843.2007.00008.x. PMID: 17214611.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/17214611\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/17214611\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eStanley, T. L., Fourman, L. T., Feldpausch, M. N., Purdy, J., Zheng, I., Pan, C. S., Aepfelbacher, J., Buckless, C., Tsao, A., Kellogg, A., Branch, K., Lee, H., Liu, C. Y., Corey, K. E., Chung, R. T., Torriani, M., Kleiner, D. E., Hadigan, C. M., \u0026amp; Grinspoon, S. K. (2019). Effects of tesamorelin on non-alcoholic fatty liver disease in HIV: a randomised, double-blind, multicentre trial. The lancet. HIV, 6(12), e821–e830.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC6981288\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC6981288\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eFalutz J, Mamputu JC, Potvin D, Moyle G, Soulban G, Loughrey H, Marsolais C, Turner R, Grinspoon S. Effects of tesamorelin (TH9507), a growth hormone-releasing factor analog, in human immunodeficiency virus-infected patients with excess abdominal fat: a pooled analysis of two multicenter, double-blind placebo-controlled phase 3 trials with safety extension data. J Clin Endocrinol Metab. 2010 Sep;95(9):4291-304. doi: 10.1210\/jc.2010-0490. Epub 2010 Jun 16. PMID: 20554713.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/20554713\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/20554713\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eTesamorelin Effects on Liver Fat and Histology in HIV.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/clinicaltrials.gov\/ct2\/show\/NCT02196831\"\u003ehttps:\/\/clinicaltrials.gov\/ct2\/show\/NCT02196831\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003ePhase II Trial of Tesamorelin for Cognition in Aging HIV-Infected Persons.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/clinicaltrials.gov\/ct2\/show\/record\/NCT02572323\"\u003ehttps:\/\/clinicaltrials.gov\/ct2\/show\/record\/NCT02572323\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eClemmons, D. R., Miller, S., \u0026amp; Mamputu, J. C. (2017). Safety and metabolic effects of tesamorelin, a growth hormone-releasing factor analogue, in patients with type 2 diabetes: A randomized, placebo-controlled trial. PloS one, 12(6), e0179538.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5472315\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5472315\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eAdrian S, Scherzinger A, Sanyal A, Lake JE, Falutz J, Dubé MP, Stanley T, Grinspoon S, Mamputu JC, Marsolais C, Brown TT, Erlandson KM. The Growth Hormone Releasing Hormone Analogue, Tesamorelin, Decreases Muscle Fat and Increases Muscle Area in Adults with HIV. J Frailty Aging. 2019;8(3):154-159. doi: 10.14283\/jfa.2018.45. PMID: 31237318; PMCID: PMC6766405.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC6766405\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC6766405\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eSivakumar T, Mechanic O, Fehmie DA, Paul B. Growth hormone axis treatments for HIV-associated lipodystrophy: a systematic review of placebo-controlled trials. HIV Med. 2011 Sep;12(8):453-62.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1111\/j.1468-1293.2010.00906.x\"\u003edoi: 10.1111\/j.1468-1293.2010.00906.x\u003c\/a\u003e. Epub 2011 Jan 25. PMID: 21265979.\u003c\/li\u003e\n\u003c\/ol\u003e\n\u003cp\u003e\u003ca title=\"Tesamorelin 10MG COA\" href=\"https:\/\/purexlabs.io\/pages\/tesamorelin-10mg-coa\"\u003eCOA\u003c\/a\u003e\u003c\/p\u003e","brand":"PureX Labs","offers":[{"title":"5mg","offer_id":48358718931188,"sku":null,"price":70.0,"currency_code":"USD","in_stock":true},{"title":"10mg","offer_id":47548295807220,"sku":null,"price":120.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0804\/5802\/3156\/files\/Render_Mockup_1920_1920_2026-01-31_2_e451d656-de7c-4087-b18e-5f114f3a1594.png?v=1769799798"},{"product_id":"sermorelin","title":"Sermorelin","description":"\u003cp dir=\"ltr\"\u003eSermorelin is a 29 amino acid peptide, the shortest synthetically developed peptide that may potentially induce biological activity at the receptors for the growth hormone-releasing hormone (GHRH).\u003csup dir=\"ltr\"\u003e(2)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eSermorelin polypeptide is an analog of the GHRH factor consisting of GHRH (1-29 acid)-amide. Due to this structural and functional mimicry, Sermorelin has been studied across multiple branches of scientific research involving growth hormone deficiency models.\u003csup dir=\"ltr\"\u003e(3)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eIt was in the early 1980s that the action of Sermorelin, classified as a growth hormone-releasing fragment GHRF (1-29) amide, was first explored. Several research studies were conducted on rats where exogenous GHRF (1-29) amide was introduced in conscious and anesthetized rats. It was observed that the presence of GHRF appeared to stimulate the pituitary gland and promote growth. Following this theory, Sermorelin and similar compounds have become the subject of further research in growth hormone deficiency models.\u003csup dir=\"ltr\"\u003e(4)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp\u003eSermorelin is suggested to be a growth hormone analog constituting the first 29 amino acids out of the usual 44 amino acids found in growth hormone-releasing hormone (GHRH). Researchers posit that Sermorelin binds with the GHRH receptors found on the pituitary gland and suggest further that the synthetic peptide may stimulate secretion of growth hormone (hGH). Thus, Sermorelin is believed to maintain the fundamental function of GHRH, possibly stimulating the GHRH receptors in the pituitary gland and leading to sporadic release of growth hormone despite its reduced amino acid sequence. This mechanism is thought to result in increased levels of insulin-like growth factor-1 (IGF-1), primarily recognized for its role in the anabolic actions of growth hormone. The estimated half-life of Sermorelin is around 11 to 12 minutes.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eA major potential advantage of the peptide is that due to its apparent GHRH receptor specificity, it may not induce any significant change in the levels of other endocrine markers such as prolactin, insulin, cortisol, glucose, or thyroid hormones.\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003eChemical Makeup\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Formula:\u003cspan\u003e \u003c\/span\u003e\u003c\/strong\u003eC\u003csub dir=\"ltr\"\u003e149\u003c\/sub\u003eH\u003csub dir=\"ltr\"\u003e246\u003c\/sub\u003eN\u003csub dir=\"ltr\"\u003e44\u003c\/sub\u003eO\u003csub dir=\"ltr\"\u003e42\u003c\/sub\u003eS\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eMolecular Weight:\u003c\/strong\u003e\u003cspan\u003e \u003c\/span\u003e3357.93 g\/mol\u003cbr dir=\"ltr\"\u003e\u003cstrong dir=\"ltr\"\u003eOther Known Titles:\u003cspan\u003e \u003c\/span\u003e\u003c\/strong\u003eGRF 1-29\u003c\/p\u003e\n\u003ch2\u003eResearch and Clinical Studies\u003c\/h2\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin and GHRH Receptors\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eSermorelin is thought to interact with GHRH receptors through complex molecular mechanisms, possibly triggering various cellular signaling pathways. It is hypothesized that upon binding to the GHRH receptor, Sermorelin may alter the receptor's structure, potentially initiating a series of intracellular signaling events.\u003csup dir=\"ltr\"\u003e(12)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eSome researchers propose that Sermorelin might enhance the production of cyclic adenosine monophosphate (cAMP) in specific cells. This enhancement may occur through the activation of adenylate cyclase, which is suggested to convert ATP into cAMP. Higher levels of cAMP might lead to the activation of protein kinase A (PKA), a key enzyme in cellular signaling processes. PKA might phosphorylate various target proteins, thereby initiating further cellular responses. The potential activation of the GHRH receptor by Sermorelin, along with the ensuing cAMP-PKA signaling cascade, is thought to possibly promote the secretion and distribution of growth hormone (hGH) from somatotroph cells in the pituitary gland. The secreted hGH is also believed to contribute to the synthesis of insulin-like growth factor-1 (IGF-1).\u003csup dir=\"ltr\"\u003e(12)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin Peptide and Growth Velocity\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eResearchers reported positive results in the idiopathic GH deficiency when Sermorelin was presented to underdeveloped animal models. Increased growth and height velocity rate was observed within 12 months of consistent, continuous peptide presence. These elevated levels were reported to be sustained for an average of 36 months after continuous presence.\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin Peptide and Anabolic Research Outcomes\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003ePreliminary findings from one investigation indicate that Sermorelin may lead to an 82% enhancement in average growth hormone levels, with actions persisting for approximately two hours.\u003csup dir=\"ltr\"\u003e(13)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eA separate study conducted over 16 weeks hypothesizes that Sermorelin might elevate growth hormone levels by as much as 107%, and increase IGF-1 levels by about 28%.\u003csup dir=\"ltr\"\u003e(14)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThe research further suggests a possible increase in lean body mass of approximately 2.78 lbs (1.26 kg), with no significant change in fat mass. These actions are tentatively attributed to the peptide's capacity to boost growth hormone levels, and in turn, IGF-1, which is considered a potential anabolic agent influencing growth hormone activity. The most noteworthy outcomes identified by the researchers include observations that there was “\u003cem dir=\"ltr\"\u003ea gain of 1.26 ± 0.52 kg (P \u0026lt; 0.05) in LBM\u003c\/em\u003e” and that “\u003cem dir=\"ltr\"\u003eskin thickness increased significantly.\u003c\/em\u003e”\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin Peptide and Lipodystrophy\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eScientists carried out a controlled clinical study involving 31 HIV-positive subjects with lipodystrophy, to investigate the potential impact of Sermorelin.\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eAll 31 subjects were divided into two groups, where one was presented with Sermorelin, and the other group with a placebo for 12 weeks. Following the study, it was suggested by the research team that growth hormone levels appeared significantly increased in Sermorelin subjects as compared to the ones given a placebo. Levels of insulin-like growth factor (IGF-1) had apparently increased – resulting in increased lean body mass in the peptide group. Abdominal visceral fat and the ratio of trunk to lower extremity fat were reported by the researchers to be significantly reduced. There was no other reported change in the glucose or insulin levels.\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin Peptide and Cognition\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eIn the early 2000s, clinical research studies were conducted with 89 subjects between 68 and 69 years of age to explore the correlation (if any) between tapering growth hormone release and impaired cognition. Scientists consider that with increasing age, levels of growth hormone naturally decline, which may result in reduced physiological functions, including cognition (i.e. ability to collect, process, and recollect information). Following the introduction of Sermorelin, it was observed that there was an apparent improved performance in the Wechsler Adult Intelligence Scale (WAIS) – i.e. improved IQ levels, picture arrangement tests, and verbal tests - amongst the test subjects.\u003csup dir=\"ltr\"\u003e(9)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin Peptide and Tumor Cells\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eA clinical study was designed where 1,018 glioma subjects were presented with over 4,000 compounds each, and following each presentation, a DRS was determined for all compounds, for each subject. Following the results of the study, it appeared that the Sermorelin compound reportedly induced the most sensitivity in the test subjects. Upon analysis, it was suggested by the researchers that this may be due to the potential of Sermorelin to block the tumor cell cycles, thereby possibly preventing tumor cell proliferation.\u003csup dir=\"ltr\"\u003e(10)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eSermorelin Peptide and Hypogonadism\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp\u003eInitial research into the peptide suggested that Sermorelin might be impactful in increasing lean mass. One study sought to explore if Sermorelin had potential in hypogonadism (which is considered to stem from additional fat mass). Test models were divided into two groups where one group was presented with Sermorelin followed by GHRH 1-40, with a one week interval between the two compounds, whereas the other group was given the same combination in reverse order. Following the study, it was reported by the researchers that for both groups, the Sermorelin appeared to stimulate the release of FSH and LH, which might stimulate testosterone production.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eThis initial research spawned additional studies, including one clinical study that included 19 male subjects, 9 of whom were aged between 22 and 33 years of age, and 10 were aged between 60 and 78 years of age. The more elderly subjects were presented with one of two concentrations of Sermorelin for a period of 28 days, with an interval of 14 days in between the two instances. Testosterone levels in the elderly subjects reportedly increased after the presentation of Sermorelin; however, it should be noted that the levels were not statistically significant. Furthermore, researchers suggested that elevated levels of growth hormones, possibly induced by Sermorelin presence, appeared to be at peak during the night time, for all test subjects, as compared during the day.\u003csup dir=\"ltr\"\u003e(11)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong dir=\"ltr\"\u003eSermorelin peptide is available for research and laboratory purposes only.\u003c\/strong\u003e\u003c\/em\u003e\u003c\/p\u003e\n\u003ch3\u003eReferences:\u003c\/h3\u003e\n\u003col\u003e\n\u003cli\u003eGarcia JM, Merriam GR, Kargi AY. Growth Hormone in Aging. [Updated 2019 Oct 7]. In: Feingold KR, Anawalt B, Boyce A, et al., editors. Endotext [Internet]. South Dartmouth (MA): MDText.com, Inc.; 2000.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK279163\/?report=reader\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/books\/NBK279163\/?report=reader\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003ePrakash, A, and K L Goa. “Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency.” BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy vol. 12,2 (1999): 139-57.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/18031173\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/18031173\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eNational Center for Biotechnology Information. \"PubChem Compound Summary for CID 16129620, Sermorelin\" PubChem\u003c\/li\u003e\n\u003cli\u003eClark, R G, and I C Robinson. “Growth induced by pulsatile infusion of an amidated fragment of human growth hormone releasing factor in normal and GHRF-deficient rats.” Nature vol. 314,6008 (1985): 281-3.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/2858818\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/2858818\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eDrugs at FDA: FDA Approved Drugs.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.accessdata.fda.gov\/scripts\/cder\/daf\/index.cfm?event=overview.process\u0026amp;ApplNo=020443\"\u003ehttps:\/\/www.accessdata.fda.gov\/scripts\/cder\/daf\/index.cfm?event=overview.process\u0026amp;ApplNo=020443\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eJunichi I. et al, Growth hormone secretagogues: history, mechanism of action, and clinical development, JSCM Rapid Communications Vol. 3 Issue 1, 09 February 2020.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" href=\"https:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1002\/rco2.9\"\u003ehttps:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1002\/rco2.9\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003ePrakash, A, and K L Goa. “Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency.” BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy vol. 12,2 (1999): 139-57.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/18031173\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/18031173\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eKoutkia, Polyxeni et al. “Growth hormone-releasing hormone in HIV-infected men with lipodystrophy: a randomized controlled trial.” JAMA vol. 292,2 (2004): 210-8.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/15249570\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/15249570\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eVitiello, Michael V et al. “Growth hormone releasing hormone improves the cognition of healthy older adults.” Neurobiology of aging vol. 27,2 (2006): 318-23.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/16399214\/\"\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/16399214\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eChang, Yuanhao et al. “A potentially effective drug for patients with recurrent glioma: sermorelin.” Annals of translational medicine vol. 9,5 (2021): 406. doi:10.21037\/atm-20-6561.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC8033379\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC8033379\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eSinha, Deepankar K et al. “Beyond the androgen receptor: the role of growth hormone secretagogues in the modern management of body composition in hypogonadal males.” Translational andrology and urology vol. 9,Suppl 2 (2020): S149-S159. doi:10.21037\/tau.2019.11.30.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7108996\/\"\u003ehttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7108996\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eZhou, F., Zhang, H., Cong, Z., Zhao, L. H., Zhou, Q., Mao, C., Cheng, X., Shen, D. D., Cai, X., Ma, C., Wang, Y., Dai, A., Zhou, Y., Sun, W., Zhao, F., Zhao, S., Jiang, H., Jiang, Y., Yang, D., Eric Xu, H., … Wang, M. W. (2020). Structural basis for activation of the growth hormone-releasing hormone receptor. Nature communications, 11(1), 5205.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1038\/s41467-020-18945-0\"\u003ehttps:\/\/doi.org\/10.1038\/s41467-020-18945-0\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eVittone, J., Blackman, M. R., Busby-Whitehead, J., Tsiao, C., Stewart, K. J., Tobin, J., Stevens, T., Bellantoni, M. F., Rogers, M. A., Baumann, G., Roth, J., Harman, S. M., \u0026amp; Spencer, R. G. (1997). Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men.\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eMetabolism: clinical and experimental\u003c\/em\u003e,\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003e46\u003c\/em\u003e(1), 89–96.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1016\/s0026-0495(97)90174-8\"\u003ehttps:\/\/doi.org\/10.1016\/s0026-0495(97)90174-8\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eKhorram, O., Laughlin, G. A., \u0026amp; Yen, S. S. (1997). Endocrine and metabolic effects of long-term administration of [Nle27]growth hormone-releasing hormone-(1-29)-NH2 in age-advanced men and women.\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003eThe Journal of clinical endocrinology and metabolism\u003c\/em\u003e,\u003cspan\u003e \u003c\/span\u003e\u003cem dir=\"ltr\"\u003e82\u003c\/em\u003e(5), 1472–1479.\u003cspan\u003e \u003c\/span\u003e\u003ca dir=\"ltr\" rel=\"noopener\" href=\"https:\/\/doi.org\/10.1210\/jcem.82.5.3943\"\u003ehttps:\/\/doi.org\/10.1210\/jcem.82.5.3943\u003c\/a\u003e\n\u003c\/li\u003e\n\u003c\/ol\u003e","brand":"PureX Labs","offers":[{"title":"5mg","offer_id":47548296528116,"sku":null,"price":40.0,"currency_code":"USD","in_stock":true},{"title":"10mg","offer_id":47548297019636,"sku":null,"price":65.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0804\/5802\/3156\/files\/Render_Mockup_1920_1920_2026-01-31_5.png?v=1769802134"},{"product_id":"cjc-1295-ipamorelin","title":"CJC-1295 + Ipamorelin","description":"\u003cp dir=\"ltr\"\u003eIpamorelin and CJC-1295 are both considered to be growth hormone secretagogues. Ipamorelin is a synthetic pentapeptide,\u003csup dir=\"ltr\"\u003e(1)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eand CJC-1295 peptide consists of 29 amino acids.\u003csup dir=\"ltr\"\u003e(2)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eIpamorelin appears to fall into a category of peptides classified as growth hormone secretagogues (GHSs). These are peptides that are assumed to stimulate the release of the growth hormones, however are not considered growth hormone releasing peptides themselves. On the other hand, CJC-1295 has also been suggested by researchers to stimulate the release of growth hormone, primarily by mimicking the actions of the naturally occurring growth hormone-releasing hormone (GHRH). Both Ipamorelin and CJC-1295 peptides have been assigned by researchers to this class, studied for similar potential actions and apparently differing only in terms of their half-life and pharmacokinetic profiles.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eCJC-1295 \u0026amp; Ipamorelin peptides both are suggested by researchers to augment the levels of the growth hormones through a possible triggering of the anterior pituitary gland. Scientists consider that once triggered, growth hormones may be naturally secreted, maintaining levels of growth hormones in the organism.\u003csup dir=\"ltr\"\u003e(3)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eCJC-1295 peptide is a tetrasubstituted version of GHRH 1-29, developed to represent the shortest functional sequence of GHRH. GHRH 1-29 consists of the first 29 amino acids of the native GHRH peptide, and may potentially stimulate growth hormone production in pituitary gland cells, called somatotrophs. The peptide has four amino acid substitutions in its structure, which scientists suggest may enhance its activity and resistance towards proteolytic enzymes. More specifically, the amino acids which are replaced appear to be the 2nd, 8th, 15th, and 27th amino acids. Owing to these substitutions, the peptide might be able to bind covalently to blood albumin, with trace amounts possibly able to bind to fibrinogen and immunoglobulin G (IgG). As a result, the apparent half-life of the peptide may increase from 10 mins to 30 mins.\u003csup dir=\"ltr\"\u003e(4)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThis may lead to elevated levels of plasma growth hormone and insulin-like growth factor 1 (IGF-1).\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eCJC-1295 might also be linked with the purported drug affinity complex (DAC) element, which may attach to plasma proteins. In particular, the DAC element in CJC-1295 alludes to the connection of N-epsilon-3-maleimidopropionamide derivative of lysine at the C-terminal end. Merging the tetrasubstituted amino acid chain and the DAC element, CJC-1295 appears to display enhanced pharmacokinetics yet retains a comparable attraction to the GHRH receptors in the pituitary gland, similar to natural GHRH.\u003csup dir=\"ltr\"\u003e(5)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eMore specifically, researchers comment that when the peptide was “\u003ci dir=\"ltr\"\u003eselected for further pharmacokinetic evaluation, where it was found to be present in plasma beyond 72 h.\u003c\/i\u003e”\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003ca title=\"Ipamorelin for Sale - 5mg\" href=\"https:\/\/www.corepeptides.com\/peptides\/ipamorelin-5mg\/\" dir=\"ltr\"\u003eIpamorelin\u003c\/a\u003e\u003cspan\u003e \u003c\/span\u003eis a man-made pentapeptide, also known as NNC 26-0161, that is believed to associate with a specific receptor in the pituitary gland cells, termed the growth hormone secretagogue receptor (GHS-R1a). These receptors are considered to be located in the hypothalamus. Moreover, GHS-R1a is often referred to as the ghrelin receptors because ghrelin seems to be its primary natural ligand. Ipamorelin appears to stand out from other GHSs as a potentially more selective compound, which may possibly stimulate the release of GH levels by somatotroph cells without also increasing other hormones produced by the anterior pituitary gland, such as prolactin.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eWhen the peptide blend, sometimes also called the peptide stack, is presented in combination, research studies typically report that the Ipamorelin exerts initial action, exhibiting some sign of impact within the first two hours of presentation, and as it starts to wean off, the CJC-1295 peptide may gradually supplement action.\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003eChemical Makeup\u003c\/h3\u003e\n\u003cp\u003e\u003cstrong\u003eMolecular Formula:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cb dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003eCJC-1295:\u003c\/em\u003e\u003c\/b\u003e\u003cem dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003eC\u003c\/em\u003e\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e152\u003c\/em\u003e\u003c\/sub\u003eH\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e252\u003c\/em\u003e\u003c\/sub\u003eN\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e44\u003c\/em\u003e\u003c\/sub\u003eO\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e42\u003c\/em\u003e\u003c\/sub\u003e\n\u003c\/li\u003e\n\u003cli\u003e\n\u003cb dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003eIpamorelin:\u003c\/em\u003e\u003c\/b\u003e\u003cem dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003eC\u003c\/em\u003e\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e38\u003c\/em\u003e\u003c\/sub\u003eH\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e49\u003c\/em\u003e\u003c\/sub\u003eN\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e9\u003c\/em\u003e\u003c\/sub\u003eO\u003csub dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003e5\u003c\/em\u003e\u003c\/sub\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eMolecular Weight:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eOther Known Titles\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cb dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003eCJC-1295:\u003c\/em\u003e\u003c\/b\u003e\u003cem dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003eCJC-1295 NO DAC; Mod GRF 1-29\u003c\/em\u003e\n\u003c\/li\u003e\n\u003cli\u003e\n\u003cb dir=\"ltr\"\u003e\u003cem dir=\"ltr\"\u003eIpamorelin:\u003c\/em\u003e\u003c\/b\u003e\u003cem dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003eNNC 26-0161\u003c\/em\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eResearch and Clinical Studies\u003c\/h2\u003e\n\u003ch3\u003e\u003cem\u003eCJC-1295 \u0026amp; Ipamorelin Blend and Half Life Determination\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eClinical studies have been conducted on test subjects to determine the half life of and individual pharmacokinetic profiles of the two peptides. In one late 1990s study,\u003csup dir=\"ltr\"\u003e(6)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ea clinical trial was conducted on eight male test subjects with a concentration escalation design. The level of growth hormones was monitored after every instance of peptide presentation. At the end of the study, it was suggested by the researchers that there was a single episode of growth hormone release with the highest peak at 0.67 hours, after which there was an exponential decline up to negligible concentrations of the compound. This study concluded that the Ipamorelin peptide appeared to exhibit a short half-life of 2 hours, after which the potential action appears to begin to decline.\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003ca title=\"CJC-1295 for Sale - 5mg\" href=\"https:\/\/www.corepeptides.com\/peptides\/cjc-1295-no-dac-mod-grf-1-29\/\" dir=\"ltr\"\u003eCJC-1295\u003c\/a\u003e, by contrast, appears to have a much longer half-life. Researchers comment that a single introduction of the peptide may upregulate growth hormone production by somatotrophs for prolonged periods of time, thus apparently contributing “\u003ci dir=\"ltr\"\u003eto an overall increase in [growth hormone] secretion … by 46%\u003c\/i\u003e” and also potentially upregulating its main anabolic mediator insulin-like growth factor-1 (IGF-1) by 45% on average.\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eAnother publication also observes that CJC-1295 may potentially upregulate “\u003ci dir=\"ltr\"\u003e[growth hormone] concentrations by 2- to 10-fold,\u003c\/i\u003e” and estimates that the half-life of the peptide ranges between 5.8 – 8.1 days.\u003csup dir=\"ltr\"\u003e(8)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eCJC-1295 \u0026amp; Ipamorelin Blend General Research\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eIn this early 2000s study,\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003ea clinical trial was conducted on male test subjects aged between 20 and 40 years old. Test subjects were divided into two groups; one group was presented with the placebo and the other with the peptide. Blood was sampled from the subjects one week before and after the presentation of CJC-1295 peptide (and placebo) to monitor the levels of growth hormone pulsatility. At the end of the study, it was suggested that CJC-1295 contributed to a 7.5-fold increase in the growth hormone pulsatility levels as compared to that of the placebo. Apart from apparently affecting the synthesis of growth hormone, scientists also suggest that CJC-1295 may interact with the survival and proliferation of the cells that synthesize it - the somatotroph cells in the anterior pituitary gland.\u003csup dir=\"ltr\"\u003e(9)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eIn one study on murine models, the authors commented that \"\u003ci dir=\"ltr\"\u003eCJC-1295 caused an increase in total pituitary RNA and GH mRNA, suggesting that proliferation of somatotroph cells had occurred, as confirmed by immunohistochemistry images.\u003c\/i\u003e”\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eTo exert these apparent effects, CJC-1295 appears to interact with specific binding sites on the GHRH receptor protein, leading to conformational changes in the receptor structure and potentially initiating a cascade of molecular events. The binding appears to activate intracellular signaling proteins that potentially act as molecular toggles.\u003csup dir=\"ltr\"\u003e(10)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eThese proteins are often referred to as G-proteins, which, upon activation, might drive the generation of secondary messengers like cyclic adenosine monophosphate (cAMP) or inositol trisphosphate (IP3.\u003csup dir=\"ltr\"\u003e(11)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eSecondary messengers such as cAMP may set in motion protein kinases, enzymes believed to alter distinct proteins. These kinases possess a modulatory capacity for cellular activities and might phosphorylate transcription regulators, or proteins overseeing gene modulation. Once phosphorylated, these transcription regulators could migrate into the nucleus of somatotroph cells, possibly impacting genes associated with growth hormone formation.\u003csup dir=\"ltr\"\u003e(7)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003eOn the other hand, Ipamorelin appears to interact with the anterior pituitary gland cells via the N-terminus of GHS-R1a, which has binding sites that appear to recognize specific sequences in the secretagogue. When Ipamorelin meets this receptor, it may attach in a non-permanent way through forces like hydrogen bonds and forces between molecules called van der Waals forces. This attachment might make the receptor change its shape, which could start cell signals, mainly those involving G-proteins. GHS-R1a might work with a specific part of G-proteins called Gαq\/11.\u003csup dir=\"ltr\"\u003e(12)\u003c\/sup\u003e\u003cspan\u003e \u003c\/span\u003eA main process started by GHS-R1a involves an enzyme called phospholipase C (PLC). Gαq\/11 interacts with PLC, which may split a fat-like molecule, phosphatidylinositol 4,5-bisphosphate (PIP2), into two messaging molecules: IP3 (Inositol trisphosphate) and DAG (Diacylglycerol). IP3 appears to attach to places on a cell part called the endoplasmic reticulum, causing calcium ions (Ca2+) to be released. Also, DAG might turn on an enzyme called protein kinase C (PKC), which may add phosphate groups to other signaling molecules. All these steps might end with the ‘turning on’ of proteins that help release growth hormone from certain cells in the pituitary gland.\u003csup dir=\"ltr\"\u003e(13)\u003c\/sup\u003e\u003c\/p\u003e\n\u003ch3\u003e\u003cem\u003eCJC-1295 \u0026amp; Ipamorelin Blend and Nitrogen Balance\u003c\/em\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003eThe apparent synergistic action of CJC-1295 and Ipamorelin on the production of growth hormone by the somatotroph cells in the anterior pituitary gland appears to result in a positive nitrogen balance and potential increase in lean mass in test models. In a particular study, investigators sought to probe the metabolic capabilities of Ipamorelin within the context of certain hepatic markers related to alpha-amino-nitrogen processing during an artificlaly triggered catabolism. The team evaluated the liver's ability to produce urea-N (CUNS), a potential metric of nitrogen processing within the liver. They examined the observable levels of messenger RNA (mRNA) linked to enzymes of the urea cycle in the liver, gauged the overall nitrogen equilibrium, and postulated the nitrogen quantities in different organs. It was proposed that Ipamorelin might have led to a 20% decline in CUNS, in contrast to the catabolic condition that was artificially prompted by the researchers. Moreover, it could have conceivably decreased the manifestation of urea cycle enzymes, reinstated nitrogen equilibrium, and theoretically adjusted or enhanced the nitrogen values in organs.\u003csup dir=\"ltr\"\u003e(14)\u003c\/sup\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem dir=\"ltr\"\u003eCJC-1295 \u0026amp; Ipamorelin peptide blend is available for research and laboratory purposes only.\u003c\/em\u003e\u003c\/strong\u003e\u003c\/p\u003e\n\u003ch3\u003eReferences:\u003c\/h3\u003e\n\u003col\u003e\n\u003cli\u003eRaun K, Hansen BS, Johansen NL, Thøgersen H, Madsen K, Ankersen M, Andersen PH. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998 Nov;139(5):552-61. doi: 10.1530\/eje.0.1390552. PMID: 9849822.\u003ca href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/9849822\/\" rel=\"noopener\" dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/9849822\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eLucie Jette et al, hGRF1-29-Albumin Bioconjugates Activate the GRF Receptor on the Anterior Pituitary in Rats: Identification of CJC-1295 as a Long Lasting GRF Analog, ResearchGate, January 2005.\u003c\/li\u003e\n\u003cli\u003eRaun K, Hansen BS, Johansen NL, Thøgersen H, Madsen K, Ankersen M, Andersen PH. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998 Nov;139(5):552-61. doi: 10.1530\/eje.0.1390552. PMID: 9849822\u003ca href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/9849822\/\" rel=\"noopener\" dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/9849822\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eThe Discovery of Growth Hormone-Releasing Hormone: An Update\u003ca href=\"https:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1111\/j.1365-2826.2008.01740.x\" rel=\"noopener\" dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003ehttps:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1111\/j.1365-2826.2008.01740.x\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eJetté, L., Léger, R., Thibaudeau, K., Benquet, C., Robitaille, M., Pellerin, I., Paradis, V., van Wyk, P., Pham, K., \u0026amp; Bridon, D. P. (2005). Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog. Endocrinology, 146(7), 3052–3058.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1210\/en.2004-1286\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1210\/en.2004-1286\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eGobburu JV, Agersø H, Jusko WJ, Ynddal L (September 1999). “Pharmacokinetic-pharmacodynamic modeling of ipamorelin, a growth hormone releasing peptide, in human volunteers”. Pharmaceutical Research. 16 (9): 1412–6. doi:10.1023\/A:1018955126402\u003c\/li\u003e\n\u003cli\u003eIonescu M, Frohman LA. Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. J Clin Endocrinol Metab. 2006 Dec;91(12):4792-7. doi: 10.1210\/jc.2006-1702. Epub 2006 Oct 3. PMID: 17018654.\u003ca href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/17018654\/\" rel=\"noopener\" dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/17018654\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eTeichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults. J Clin Endocrinol Metab. 2006 Mar;91(3):799-805. doi: 10.1210\/jc.2005-1536. Epub 2005 Dec 13. PMID: 16352683.\u003ca href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/16352683\/\" rel=\"noopener\" dir=\"ltr\"\u003e\u003cspan\u003e \u003c\/span\u003ehttps:\/\/pubmed.ncbi.nlm.nih.gov\/16352683\/\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eAlba, M., Fintini, D., Sagazio, A., Lawrence, B., Castaigne, J. P., Frohman, L. A., \u0026amp; Salvatori, R. (2006). Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse.\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003eAmerican journal of physiology. Endocrinology and metabolism\u003c\/i\u003e,\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003e291\u003c\/i\u003e(6), E1290–E1294.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1152\/ajpendo.00201.2006\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1152\/ajpendo.00201.2006\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eMartin, B., Lopez de Maturana, R., Brenneman, R., Walent, T., Mattson, M. P., \u0026amp; Maudsley, S. (2005). Class II G protein-coupled receptors and their ligands in neuronal function and protection.\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003eNeuromolecular medicine\u003c\/i\u003e,\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003e7\u003c\/i\u003e(1-2), 3–36.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1385\/nmm:7:1-2:003\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1385\/nmm:7:1-2:003\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eNewton, A. C., Bootman, M. D., \u0026amp; Scott, J. D. (2016). Second Messengers.\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003eCold Spring Harbor perspectives in biology\u003c\/i\u003e,\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003e8\u003c\/i\u003e(8), a005926.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1101\/cshperspect.a005926\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1101\/cshperspect.a005926\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eYin, Y., Li, Y., \u0026amp; Zhang, W. (2014). The growth hormone secretagogue receptor: its intracellular signaling and regulation.\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003eInternational journal of molecular sciences\u003c\/i\u003e,\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003e15\u003c\/i\u003e(3), 4837–4855.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.3390\/ijms15034837\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.3390\/ijms15034837\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eBill, C. A., \u0026amp; Vines, C. M. (2020). Phospholipase C.\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003eAdvances in experimental medicine and biology\u003c\/i\u003e,\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003e1131\u003c\/i\u003e, 215–242.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1007\/978-3-030-12457-1_9\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1007\/978-3-030-12457-1_9\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli\u003eAagaard, N. K., Grøfte, T., Greisen, J., Malmlöf, K., Johansen, P. B., Grønbaek, H., Ørskov, H., Tygstrup, N., \u0026amp; Vilstrup, H. (2009). Growth hormone and growth hormone secretagogue effects on nitrogen balance and urea synthesis in steroid treated rats.\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003eGrowth hormone \u0026amp; IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society\u003c\/i\u003e,\u003cspan\u003e \u003c\/span\u003e\u003ci dir=\"ltr\"\u003e19\u003c\/i\u003e(5), 426–431.\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1016\/j.ghir.2009.01.001\" rel=\"noopener\" dir=\"ltr\"\u003ehttps:\/\/doi.org\/10.1016\/j.ghir.2009.01.001\u003c\/a\u003e\n\u003c\/li\u003e\n\u003c\/ol\u003e","brand":"PureX Labs","offers":[{"title":"10mg","offer_id":47548298002676,"sku":null,"price":50.0,"currency_code":"USD","in_stock":false},{"title":"20mg","offer_id":48318298063092,"sku":null,"price":100.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0804\/5802\/3156\/files\/Render_Mockup_1920_1920_2026-01-31_7.png?v=1769804832"},{"product_id":"cjc-1295","title":"CJC-1295","description":"\u003cp data-end=\"505\" data-start=\"188\"\u003eCJC-1295 is a synthetic 29–amino acid analog of growth hormone–releasing hormone (GHRH) designed to stimulate the pituitary gland to release endogenous growth hormone (GH). It represents the shortest functional fragment of GHRH capable of activating somatotroph cells, which are responsible for GH production.\u003c\/p\u003e\n\u003cp data-end=\"820\" data-start=\"507\"\u003eThe peptide contains four amino acid substitutions compared to native GHRH. These modifications are theorized to enhance stability, receptor affinity, and resistance to enzymatic degradation, resulting in a longer functional duration than natural GHRH while preserving physiological, pulsatile GH release.\u003c\/p\u003e\n\u003cp data-end=\"1203\" data-start=\"822\"\u003eBy binding to GHRH receptors, CJC-1295 is believed to activate intracellular signaling pathways involving G-proteins and secondary messengers such as cAMP, which may promote GH gene expression. Increased GH secretion may subsequently elevate insulin-like growth factor-1 (IGF-1) levels, a hormone associated with protein synthesis, tissue growth, and cellular regeneration.\u003c\/p\u003e\n\u003cp data-end=\"1489\" data-start=\"1205\"\u003eCJC-1295 has been studied for its potential role in lean muscle support, fat metabolism, bone and connective tissue maintenance, and sleep-related neuroendocrine function. Due to its modified structure, it is reported to have a longer half-life (~30 minutes) than native GHRH.\u003c\/p\u003e\n\u003cp data-end=\"1558\" data-start=\"1491\"\u003eCJC-1295 is intended for research and laboratory purposes only.\u003c\/p\u003e","brand":"PureX Labs","offers":[{"title":"5mg","offer_id":47548299084020,"sku":null,"price":35.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0804\/5802\/3156\/files\/Render_Mockup_1920_1920_2026-01-31_8.png?v=1769804832"}],"url":"https:\/\/purexlabs.io\/collections\/growth-hormone.oembed","provider":"PureX Labs","version":"1.0","type":"link"}