This is a working overview of GHRH receptor, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2026-03-30 and is reviewed periodically as new material appears.
CJC-1295 is a synthetic peptide analog of growth hormone-releasing hormone, constructed on the 29-amino-acid fragment designated GRF(1-29). The name began as an internal development code during the 1990s and later spread through research supply catalogs and discussion forums. The molecule does not occur in nature; its sequence is engineered rather than isolated from tissue. Two related compounds are sold under this single label, and they differ by one appended chemical group that strongly influences how long the peptide remains in circulation.
The dividing feature between the two forms is a maleimide-based drug affinity complex, abbreviated DAC. In the DAC-bearing version, a linker attaches the peptide to serum albumin after administration, and that association slows removal from plasma. The version lacking DAC appears in catalogs as MOD GRF(1-29) or tetrasubstituted GRF(1-29). Because informal writing treats both as one item, comparisons drawn from such sources routinely blend measurements taken from two molecules with substantially different behavior.
The attached maleimide group explains the unusual duration of the DAC version. After injection it reacts with the thiol of cysteine-34 on serum albumin, forming a stable covalent bond. The resulting conjugate is too large for rapid kidney filtration and is shielded from many peptidases. Reported half-lives for this form reach several days, whereas the version without the group is cleared in roughly half an hour. That gap is the main pharmacological difference between the two.
Downstream of growth hormone, the liver and other tissues increase production of insulin-like growth factor 1, a mediator of many growth-promoting effects. Studies have documented elevated levels of both hormones after dosing, and the rise from the long-acting form persists longer than that produced by shorter-acting analogues. What remains unclear is whether sustained elevation of these markers translates into meaningful clinical benefit, and whether prolonged exposure carries risks that short trials could not detect.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic peptide | Analog of growth hormone-releasing hormone |
| Chain length | 29 amino acids | Based on the GRF(1-29) fragment |
| Appearance | White to off-white lyophilized powder | Common research supply form |
| Solubility | Soluble in water and aqueous buffers | Powder requires reconstitution before use |
| Typical storage | −20 °C or below | Kept away from light and moisture |
CJC-1295 is a synthetic peptide modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. Its sequence corresponds to the first twenty-nine residues of human GHRH, with four substitutions that slow enzymatic breakdown. Early descriptions placed the compound in research on growth hormone deficiency and related conditions, and later literature groups it with the long-acting GHRH analogs. The name appears in both laboratory and popular fitness writing, where it sometimes labels chemically different peptides.
Two related peptides circulate under the CJC-1295 label, and they differ mainly in how long they persist in circulation. The version carrying a drug affinity complex includes a maleimidopropionic acid linker that forms a covalent bond with serum albumin. The other version, usually written as modified GRF(1-29) or tetrasubstituted GRF(1-29), lacks that linker and is cleared quickly. Mixing the two produces inconsistent readings of published half-life values, because the linker rather than the receptor-facing sequence drives most of the difference.
The core sequence keeps the receptor-binding region of GHRH while replacing four positions that are vulnerable to dipeptidyl peptidase-4 and other proteases. Substitutions at positions 2, 8, 15, and 27 raise metabolic stability relative to the natural hormone. The N-terminal residues remain essential for activity, so changes there generally lower potency. Molecular weight sits near 3368 daltons for the tetrasubstituted analog without the linker, while the albumin-binding form is heavier because of the added maleimide group.
The distinguishing feature of the DAC form is a maleimide-containing group that reacts with the free thiol of cysteine-34 on human serum albumin. This reaction forms a covalent bond without enzymatic assistance, and it takes place after the peptide enters the bloodstream. Because albumin is abundant and long-lived, the attached peptide is carried through circulation far longer than an unmodified fragment would survive. The chemistry is a deliberate pharmacokinetic strategy rather than a change to receptor activity.
Enzymatic protection is a separate mechanism from plasma protein binding. The four substitutions in the backbone reduce recognition by dipeptidyl peptidase IV, which normally cleaves the natural hormone within minutes. Without the reactive group, this resistance still yields only a short window of activity, generally reported in the range of tens of minutes. With it, reported half-lives in early human work extended to several days. The size of that gap is the main practical distinction between the two materials.
Both forms act at the pituitary receptor for growth hormone-releasing hormone and increase growth hormone output, which in turn raises insulin-like growth factor 1. A long-acting analog produces sustained rather than pulsatile stimulation, and the physiological consequences of that pattern are not fully settled. Published human data on the extended form remain limited, and much of what circulates in discussion traces to early company reports rather than independent replication. How sustained exposure affects normal feedback remains an open question.
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An amphibolic pathway is one that can be either catabolic or anabolic based on the availability of or the need for energy. The currency of energy in a biological cell is adenosine triphosphate (ATP), which stores its energy in the phosphoanhydride bonds. The energy is utilized to conduct biosynthesis, facilitate movement, and regulate active transport inside of the cell. Examples of amphibolic pathways are the citric acid cycle and the glyoxylate cycle. These sets of chemical reactions contain both energy producing and utilizing pathways. To the right is an illustration of the amphibolic properties of the TCA cycle. The glyoxylate shunt pathway is an alternative to the tricarboxylic acid (TCA) cycle, for it redirects the pathway of TCA to prevent full oxidation of carbon compounds, and to preserve high energy carbon sources as future energy sources. This pathway occurs only in plants and bacteria and transpires in the absence of glucose molecules.
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Sources: en.wikipedia.org
No. It is a laboratory-synthesized analog built on a fragment of the natural hormone. The natural peptide is shorter-lived and lacks the stabilizing substitutions found in the synthetic version.
DAC stands for drug affinity complex, a chemical group that binds the peptide to serum albumin. The binding slows clearance and lengthens the time the molecule stays in plasma compared with the unmodified analog.
Because two distinct molecules are discussed under one informal label. The albumin-binding version clears over several days, while the form without that group clears within roughly half an hour. Mixing results from both creates inconsistent figures.
It binds the growth hormone-releasing hormone receptor on pituitary somatotroph cells. Receptor activation raises cyclic AMP and promotes release of stored growth hormone granules. Because the peptide persists longer than natural releasing hormone, stimulation is prolonged rather than brief.