Mod GRF 1-29 (CJC-1295 NO DAC) – 5MG

Mod GRF 1-29 (CJC-1295 NO DAC)

CJC-1295 is a synthetic peptide variation of the hormone GHRH, and it consists of 29 amino acids. This peptide is also known as Modified GRF (1-29) or CJC 1295 no DAC Its a structure containing four amino groups replaced out with other groups, which are thought to protect the original peptide from degradation. CJC no DAC is a modification of sermorelin having more strong biological effect, with a half-life extended compared to IK-2 (29 - 30 min), because of adding protection cation complex "Drug affinity complex" (DAC) does not have.

The initial discovery of modified (1-29) was in the early 1980s when a fragment of natural growth hormone-releasing hormone, GHRH(1-44), which is approximately less than one-third of its size, had shown to retain specific high-affinity binding and agonist activity on specific receptors. The half-life related to growth hormone-releasing peptides which have been created synthetically is a potential limitation. Extensive scientific research has translated into a so-called stabilized, long-lasting CJC-1295 (No DAC) peptide.

CJC-1295 without DAC which is sometimes known as the tetrasubstituted GRF (1-29) or simply CJC-1295, is the bio-conjugated version of the growth hormone-releasing hormone (GHRH), a naturally occurring peptide hormone that stimulates the release of endogenous growth hormone. Some scholars have suggested that it helps in the process of GH (growth hormone) secretion. MK-677 is designed, in making a long story short, to be made up of the most basic sequence of amino acids that can bind to GHRH receptors (in this case 29) The main structural distinctions between CJC-1295 without DAC and the unmodified fragment are four amino acids; GHRH itself was only 29 amino acids in length. Include altering the position of amino aids-2nd, 8th, 15th and 27th to improve the peptide against enzymatic breakdown or by enzymes like dipeptidyl peptidase-4 (DPP-4).

This entails, among others:
- Alignment at the 2nd position (d-alanine replaces l-alanine; believed to enhance resistance to enzymic degradation).
- More or less, the availability of increasing glutamine at the 8th locus to thwart possible asparagine reconfiguration and, amide hydrolysis.
- An exchange of a glycine with an alanine at position 15, expected to have elevated bioactivity.
- Was the change of amino acid from methionine to leucine in the 27th position and it's supposed protection against the oxidation of methionine.

THE CONTENT ON THIS WEBSITE IS STRICTLY INFORMATIONAL. IT IS NOT INTENDED TO BE TAKEN AS MEDICAL ADVICE OR AS A SCIENTIFIC PUBLICATION.

None of the products have been evaluated by The Food and Drug Administration, and are not for medical use. Their use in human or animal subjects is strictly prohibited by law, and they are available here only for in-vitro research purposes, by licensed professionals. By purchasing from this site, you agree to comply with our Terms and Conditions.