Selective Androgen Receptor Modulators (SARMs) are a class of androgen receptor ligands that bind androgen receptor and display tissue-selective activation of androgenic signaling. The initial efforts to develop steroidal SARMs, based on modifications of the testosterone molecule, date back to the 1940s. The modern era of nonsteroidal SARMs was unleashed by independent work at Ligand Pharmaceuticals and the University of Tennessee. The scientists at Ligand Pharmaceuticals were the first to develop a series of cyclic quinolinones that had anabolic activity on the skeletal muscle and some degree of tissue selectivity. The discovery by Dalton and Miller that aryl propionamides with structural similarities to bicalutamide and hydroxyflutamide could activate AR-dependent transcriptional activity provided the early lead for the development of diaryl propionamide class of SARMs.
CJC-1295 DACandCJC-1295(also known asModified GRF 1-29 are both Growth Hormone Releasing Hormones (GHRH). Their action in the human body is identical but the difference between the two peptides are the span of the half-life. Modified GRF 1-29 and Sermorelin have a very short acting half-life of about 30 minutes, while CJC-1295 DAC has a half-life that can last up to approximately 8 days. Many a scientist have reported that the short half-life ofSermorelinand Modified GRF 1-29 is considered to be much more natural as they produce a short pulse of Human Growth Hormone.
Modified Growth Releasing Factor aminos 1-29, usually referred to as Modified GRF (1-29) or “ModGRF(1-29),” also known as CJC-1295 without DAC, is a synthetic analog of the endogenous peptide signaling hormone Growth Hormone Releasing Hormone (GHRH). Endogenously producedGHRHhas 44 amino acids in its chain structure. A truncated synthetic form of GHRH calledSermorelinor GRF 1-29 has 29 amino acids; Modified GRF (1-29) is further changed in that it has four substituted aminos in its chain that serve the purposes of preventing degradation and oxidation in manufacture and transport as well as in vivo, while also increasing binding affinity to the GHRH receptors.