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Tesamorelin – Mod GRF – Ipamorelin Blend (12mg)
Tesamorelin & Mod GRF & Ipamorelin blend is Synthesized and Lyophilized in the USA.
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(Required for reconstitution)
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What is Tesamorelin & Mod GRF & Ipamorelin blend?
Tesamorelin & Mod GRF & Ipamorelin blend is a combination of peptides that appear to potentially interact with receptors in the pituitary gland and may activate pituitary cells responsible for growth hormone (HGH) production.
Tesamorelin is a synthetic peptide that appears to act as a growth hormone-releasing hormone (GHRH) analog. It may interact with specific receptors in the pituitary and the hypothalamus, known as GHRH receptors, which appear to trigger a release of growth hormone from pituitary cells.
Mod GRF (Modified Growth Hormone-Releasing Factor), also known as CJC-1295 without DAC (Drug Affinity Complex), is a synthetic peptide analog of the endogenous growth hormone-releasing hormone (GHRH). It is a tetrasubstituted version of the shortest GHRH sequence, which still appears to trigger the GHRH receptors – GRF (1-29). Thus, it appears to bind to GHRH receptors in the pituitary cells associated with the release of HGH.
Ipamorelin is another synthetic peptide that may interact with pituitary cells, although it appears to do so by triggering a different receptor called the growth-hormone secretagogue (GHS) receptor. These receptors, also called ghrelin receptors, are apparently found in the pituitary and the hypothalamus. By activating these receptors, Ipamorelin may potentially trigger the synthesis of HGH by pituitary cells.
Tesamorelin Molecular Formula: C223H370N72O69S
Mod GRF Molecular Formula: C152H252N44O42
Ipamorelin Molecular Formula: C38H49N9O5
Tesamorelin Molecular Weight: 5195.908 g/mol
Mod GRF Molecular Weight: 3367.954 g/mol
Ipamorelin Molecular Weight: 711.868 g/mol
Tesamorelin Sequence: YADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARL
Mod GRF Sequence: YDADAIFTQSYRKVLAQLSARKL LQDILSR-NH2
Ipamorelin Sequence: Aib-His-D-2Nal-D-Phe-Lys
Tesamorelin & Mod GRF & Ipamorelin Research and Clinical Studies
Tesamorelin & Mod GRF & Ipamorelin and the GHRH Receptors
The Tesamorelin & Mod GRF & Ipamorelin blend appears to act primarily via the GHRH receptors in the central nervous system, particularly the pituitary cells (somatotrophs) found in the anterior part of the gland. More specifically, the Tesamorelin & Mod GRF appear to be the two main activators of these receptors. Tesamorelin appears to have an affinity to the GHRH receptors due to its chain composed of 44 amino acids, which include the specific sequence of GHRH, also made of 44 amino acids. Yet, Tesamorelin also has an acetyl group (CH₃CO-) attached to the N-terminus, which may potentially enhance the stability and bioactivity of the peptide. Furthermore, the C-terminus of Tesamorelin has been modified with a trans-3-hexenoic acid group. This modification, known as an omega-amino acid modification, may help improve the peptide’s resistance to enzymatic degradation.
On the other hand, Mod GRF has affinity due to its apparent similarity to the shortest functional part of the GHRH – GHF (1-29). Yet it is modified at four positions – position two, eight, fifteen, and twenty-seven. At position two, the amino acid alanine (Ala) is replaced with a modified amino acid called D-Alanine (D-Ala). This substitution may potentially increase the resistance of the peptide to enzymatic degradation and improve its stability. Further, the amino acid asparagine (Asn) at position eight is replaced with a modified amino acid called Lysine (Lys). This substitution may enhance the peptide’s binding affinity to the GHRH receptor. At position fifteen, the amino acid histidine (His) is replaced with a modified amino acid called D-Phenylalanine (D-Phe). This substitution may improve the peptide’s resistance to enzymatic degradation and enhance its stability. Finally, the amino acid cysteine (Cys) at position twenty-seven is replaced with a modified amino acid called N-Methylglycine (Sar). This substitution may increase the half-life of the peptide by protecting it from enzymatic cleavage and degradation.
Tesamorelin & Mod GRF may potentially interact with the GHRH receptors via complex molecular mechanisms, which involve subsequent activation of signaling pathways. It is suggested that upon binding to the GHRH receptor, Tesamorelin & Mod GRF may induce conformational changes in the receptor structure, potentially activating intracellular signaling pathways. It is speculated that Tesamorelin & Mod GRF may stimulate the production of cyclic adenosine monophosphate (cAMP) within the target cells. This might be achieved by activating the adenylate cyclase, which may convert ATP to cAMP. It is believed that increased cAMP levels may activate protein kinase A (PKA), which appears to be a key intracellular signaling molecule. It may potentially phosphorylate various target proteins, thus initiating downstream cellular responses. The potential activation of the GHRH receptor by Tesamorelin & Mod GRF and the potential cAMP-PKA signaling cascade may stimulate HGH synthesis and secretion from somatotrophs in the pituitary gland. The HGH released from pituitary cells may also influence the synthesis of insulin-like growth factor-1 (IGF-1). Scientists also comment that IGF-1 may have a “GH independent growth stimulating effect, which with respect to cartilage cells is possibly optimized by the synergistic action with GH.“
Tesamorelin & Mod GRF & Ipamorelin and the GHS Receptors
Tesamorelin & Mod GRF & Ipamorelin blend may also have the potential to interact with the GHS receptors, particularly through the proposed mechanism of action of Ipamorelin. Researchers suggest that Ipamorelin exhibits selectivity by targeting the GHS receptor without significant cross-reactivity with other receptors. The scientists also commented, “Very surprisingly, Ipamorelin did not release ACTH or cortisol in levels significantly different from those observed following GHRH stimulation.” This apparent selectivity may allow Ipamorelin to potentially stimulate growth hormone release by pituitary cells without necessarily triggering the release of cortisol or adrenocorticotropic hormone (ACTH). Cortisol and ACTH are hormones potentially involved in the stress response and are typically associated with various metabolic and immune effects.
In vitro studies suggest that by interacting with the GHS receptors, Ipamorelin may act on somatotroph cells in the anterior pituitary gland, which may activate various intracellular signaling pathways. One such potential pathway involves the activation of phospholipase C (PLC), which researchers suggest may lead to the possible release of inositol triphosphate (IP3) and diacylglycerol (DAG). IP3 may trigger the release of calcium ions (Ca2+) from intracellular stores, while DAG may activate protein kinase C (PKC). The potential elevation of intracellular calcium levels and PKC activation may lead to the apparent exocytosis of growth hormone-containing vesicles from pituitary cells.
- Clinical Review Report: Tesamorelin (Egrifta) [Internet]. Ottawa (ON): Canadian Agency for Drugs and Technologies in Health; 2016 Aug. 1, Introduction. Available from: https://www.ncbi.nlm.nih.gov/books/NBK539137/
- Jetté, L., Léger, R., Thibaudeau, K., Benquet, C., Robitaille, M., Pellerin, I., Paradis, V., van Wyk, P., Pham, K., & 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. https://doi.org/10.1210/en.2004-1286
- Johansen, P. B., Nowak, J., Skjaerbaek, C., Flyvbjerg, A., Andreassen, T. T., Wilken, M., & Orskov, H. (1999). Ipamorelin, a new growth-hormone-releasing peptide, induces longitudinal bone growth in rats. Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society, 9(2), 106–113. https://doi.org/10.1054/ghir.1999.9998
- Spooner, L. M., & Olin, J. L. (2012). Tesamorelin: a growth hormone-releasing factor analogue for HIV-associated lipodystrophy. The Annals of pharmacotherapy, 46(2), 240–247. https://doi.org/10.1345/aph.1Q629
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- Laron Z. (2001). Insulin-like growth factor 1 (IGF-1): a growth hormone. Molecular pathology : MP, 54(5), 311–316. https://doi.org/10.1136/mp.54.5.311
- Raun, K., Hansen, B. S., Johansen, N. L., Thøgersen, H., Madsen, K., Ankersen, M., & Andersen, P. H. (1998). Ipamorelin, the first selective growth hormone secretagogue. European journal of endocrinology, 139(5), 552–561. https://doi.org/10.1530/eje.0.1390552
- Jiménez-Reina, L., Cañete, R., de la Torre, M. J., & 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. https://doi.org/10.14670/HH-17.707
Dr. Usman (BSc, MBBS, MaRCP) completed his studies in medicine at the Royal College of Physicians, London. He is an avid researcher with more than 30 publications in internationally recognized peer-reviewed journals. Dr. Usman has worked as a researcher and a medical consultant for reputable pharmaceutical companies such as Johnson & Johnson and Sanofi.