The short version of GHRH analog fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2025-08-31. Anything still debated is marked as such rather than presented as settled.
CJC-1295 is a synthetic peptide designed to mimic growth hormone-releasing hormone (GHRH), the endogenous signal that prompts the pituitary gland to release growth hormone. The compound is a modified fragment of the natural hormone, spanning the first twenty-nine amino acids of GHRH with several substitutions that slow enzymatic breakdown. Two variants circulate in research settings: one carrying a drug affinity complex (DAC) and one without it. The DAC-free form is frequently labelled Mod GRF(1-29) in catalogs and discussion forums.
The peptide binds GHRH receptors on somatotroph cells within the anterior pituitary, triggering a signalling cascade that increases growth hormone secretion. Its improved resistance to dipeptidyl peptidase IV degradation distinguishes it from the parent hormone. In the DAC-bearing version, a maleimide group reacts with a cysteine residue on serum albumin, forming a covalent bond that keeps the peptide in circulation far longer. That albumin attachment is the central design feature separating the two research variants.
Reverse-phase high-performance liquid chromatography is the standard tool for purity assessment. The technique separates the target peptide from truncated or modified byproducts. Mass spectrometry confirms molecular weight and supports sequence verification. Electrospray ionization and matrix-assisted laser desorption are both used. Amino acid analysis provides an independent check on composition. Purity values are commonly reported as area percentage from the chromatogram. Residual trifluoroacetate and water content are also measured in many quality programs.
Batch-to-batch consistency depends on solid-phase peptide synthesis and subsequent purification. Coupling efficiency, resin choice, and cleavage conditions all affect the final profile. Counter-ion content and moisture can shift the apparent mass of a batch. Documentation typically includes a certificate of analysis with chromatograms and spectra. Independent verification by a second laboratory is sometimes requested. Whether a given certificate reflects the actual vial contents depends on chain of custody. Analytical methods themselves carry uncertainty that should be stated alongside results.
| Property | Value | Notes |
|---|---|---|
| Molecular weight (with DAC) | ~3647 Da | Calculated from the full amino acid sequence |
| Molecular weight (without DAC) | ~3368 Da | Mod GRF(1-29) variant |
| Appearance | White lyophilized powder | Typical form supplied for research |
| Solubility | Soluble in water | Dissolves in aqueous buffers |
| Receptor target | GHRH receptor | Expressed on pituitary somatotroph cells |
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.
Lyophilized peptide powder is comparatively stable when kept dry, cold, and protected from light. Once dissolved, the molecule is vulnerable to deamidation, oxidation, and aggregation, with the rate depending on pH, buffer composition, and temperature. Alkaline conditions and repeated freeze-thaw cycles accelerate loss of the intact peptide. The methionine present in the native sequence is a known oxidation site, which is one reason it was replaced in the modified fragment. Suppliers typically recommend cold storage of solutions and use within a short window.
Analytical confirmation usually relies on reversed-phase high-performance liquid chromatography for purity and on liquid chromatography coupled to mass spectrometry for identity. Mass data reveal the expected molecular mass and can flag truncated or oxidized species. Amino acid analysis and peptide mapping provide sequence-level verification. Immunoassays are used in some biological matrices, but antibodies raised against one releasing-hormone analog may cross-react with another. Reported purity figures depend heavily on the method used, so comparisons between suppliers require matching the analytical approach.
The two variants differ dramatically in how long they persist in circulation. The form lacking the albumin-binding group has a plasma half-life measured in tens of minutes, comparable to the natural hormone fragment. The version carrying the drug affinity complex binds albumin and shows a half-life of roughly six to eight days in human studies. That figure comes from small trials that tracked hormone levels over extended periods. The physiological consequences of sustained versus pulsatile stimulation are still debated and the literature does not settle the point.
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The panel has come to some controversy, however; on July 20, 2010, one of the panelists was discovered to have been a paid speaker for GlaxoSmithKline, arousing questions of a conflict of interest. This panel member was one of the three who voted to keep Avandia on the market with no additional warning labels. In 2011 the FDA has decided on revising its prescribing information and medication guides for all rosilitazone containing medicines. The US label for rosiglitazone (Avandia, GlaxoSmithKline) and all rosiglitazone-containing medications (Avandamet and Avandaryl) now include the additional safety information and restrictions. The revised labels restrict use to patients already taking a rosiglitazone-containing medicine or to new patients who are unable to achieve adequate glycemic control on other diabetes medications and to those, who in consultation with their healthcare provider, have decided not to take Actos (pioglitazone) or other pioglitazone-containing medicines for medical reasons. In June 2013 an FDA Advisory Committee reviewed all available data, including a re-adjudicated RECORD trial, found no evidence of increased cardiovascular risk with Avandia, and voted to remove the restrictions on Avandia marketing in the United States. In November 2013, the US FDA removed these marketing restrictions on the product. Under the FDA's instruction, Avandia's maker, GlaxoSmithKline, had funded the Duke Clinical Research Institute to re-analyze the raw data from the study.
ATP + NH3 + CO2 ⇌ ADP + H2N−C(=O)−O−PO2−3 An important example of an enzyme with this activity is carbamoyl phosphate synthetase, e.g. carbamoyl phosphate synthetase I carrying out the first step of the urea cycle in order to dispose of waste ammonia. One hemoglobin molecule can carry four molecules of carbon dioxide to the lungs as carbamate groups formed by reaction of CO2 with four terminal amine groups of the deoxy form. The resulting compound is called carbaminohaemoglobin.
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Sources: en.wikipedia.org
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=== Professional services === He has fulfilled roles in numerous professional organizations, including the Swedish Biochemical Society (secretary 1976–1982); Chairman of the Swedish National Committee on Biochemistry, Royal Swedish Academy of Sciences, 1988–1990; Chairman Scientific Program Committee for the 22nd Meeting of the Federation of European Biochemical Societies, FEBS 1993; editorial boards of the Biochemical Journal, ChemBioChem, Biochimica et Biophysica Acta, Protein Engineering Design and Selection, the Journal of Biological Chemistry. In addition, he has had advisory roles at various companies: Telik Inc.; PanVera Corporation, Pharmacia Biotech; Uniroyal Chemical Company; Biovitrum AB; Maxygen; Vividion; Oxford Biomedical Research, Rochester Hills, Michigan.
Sources: en.wikipedia.org
The synthetic peptide keeps the receptor-binding region of GHRH but carries substitutions that resist enzymatic cleavage. In the DAC version, an added group also anchors the molecule to albumin, extending its presence in the bloodstream.
The maleimide group forms a covalent link with albumin, an abundant blood protein. This attachment slows clearance, so a single administration persists much longer than the unmodified peptide. The feature is the main reason the two variants are handled differently in study design.
It is not an approved therapeutic product in major regulatory jurisdictions. It appears in research chemical catalogs and scientific literature rather than pharmacy shelves. Clinical development was limited and did not reach approval.
The powder is normally held at minus twenty degrees Celsius or below. Light and moisture exposure should be minimized. Repeated warming and cooling cycles are avoided.