If you have been reading about GHRH analog and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2026-06-17. Numbers and descriptions here follow the published literature rather than marketing material.
Two related forms appear under the CJC-1295 name. The simpler analogue, commonly written as modified GRF(1-29), carries the four substitutions but no additional conjugation. The second form attaches a maleimidopropionic acid linker to a lysine residue, a modification frequently called the drug affinity complex. That linker reacts with the free thiol on serum albumin to form a covalent bond. Because albumin has a long residence time in blood, the conjugated peptide stays in circulation far longer than the unconjugated analogue.
Receptor level activity follows the canonical GHRH pathway. The peptide binds the GHRH receptor, a class B G protein coupled receptor on somatotroph cells of the anterior pituitary. Binding raises intracellular cyclic AMP, which promotes calcium entry and the release of growth hormone into the bloodstream. Because the molecule acts at the same receptor as the endogenous hormone, its effect is superimposed on the natural pulsatile rhythm rather than replacing it. Whether sustained receptor occupation leads to desensitization is not fully settled.
CJC-1295 belongs to a class of synthetic peptides modeled on growth hormone releasing hormone, a forty-four amino acid signal produced by the hypothalamus. The compound is built from the first twenty-nine residues of the natural sequence, with four substitutions introduced at positions 2, 8, 15 and 27. These changes were designed to slow enzymatic breakdown while preserving receptor activation. The result is a peptide that is shorter than native GHRH and considerably more resistant to ordinary clearance pathways in circulation.
Identity and purity are established with reversed phase high performance liquid chromatography coupled to mass spectrometry. The chromatographic step separates the target peptide from truncated sequences and deletion products, while the mass measurement confirms the expected molecular weight to within a fraction of a dalton. Because the two common variants differ by the presence of the linker, mass alone can distinguish them in the unconjugated state. Amino acid analysis and peptide mapping are used when sequence level confirmation is required.
Lyophilized material is generally stable for extended periods when held at minus twenty degrees Celsius or below and protected from moisture and light. In solution the peptide is more labile; bond hydrolysis, aggregation and oxidation of susceptible residues all proceed faster at ambient temperature. Repeated freeze and thaw cycles should be avoided because they promote clumping and loss of soluble material. The conjugated variant adds a further consideration, since the maleimide group can hydrolyze in aqueous buffer and lose its ability to react with albumin.
Laboratory handling centers on minimizing exposure to water, heat and oxygen before use. Working solutions are typically prepared in sterile water or a mild buffer, and any residual particulate matter is removed by filtration. When the powder dissolves slowly, a small proportion of acetonitrile or dilute acetic acid is sometimes added as a co-solvent. Containers are kept sealed and desiccated between uses. Records of lot number, reconstitution date and storage conditions support later comparison of results across experiments.
| Property | Value | Notes |
|---|---|---|
| Peptide class | Synthetic GHRH analogue | Built on a 29 residue sequence |
| Primary target | GHRH receptor (GHRHR) | Class B G protein coupled receptor |
| Unconjugated half life | Minutes | Limited by protease degradation |
| Key modification | Four residue substitutions | Positions 2, 8, 15 and 27 |
| Common synonym | Modified GRF(1-29) | Usually denotes the form without DAC |
CJC-1295 is a synthetic peptide belonging to the growth hormone-releasing hormone analog family. It comprises twenty-nine amino acid residues derived from the N-terminal region of natural GHRH. The molecule incorporates several non-natural substitutions that increase resistance to enzymatic degradation. These modifications extend its activity compared with the native hormone fragment. Researchers use it to study pituitary growth hormone secretion in laboratory and clinical settings. This compound is distinct from native GHRH in its stability profile.
Two principal forms appear in the literature and in research supply. One carries a drug affinity complex, a maleimide-based group that forms a covalent bond with circulating albumin. This linkage slows clearance and produces a long-lasting elevation of peptide levels. The other form lacks that group and is often labeled MOD GRF(1-29). It has a much shorter circulation time. Both variants retain the same core receptor-binding sequence. Reported half-lives differ substantially between the two.
At the pituitary, the peptide binds the growth hormone-releasing hormone receptor on somatotroph cells. Receptor activation raises intracellular cyclic AMP and triggers release of stored growth hormone. Somatostatin and other hypothalamic signals modulate this response. Negative feedback from insulin-like growth factor 1 also influences output. The same regulatory architecture operates with the native hormone. Whether the synthetic analog alters feedback dynamics over repeated exposure remains an open question. Most published receptor work uses cell models rather than intact human systems.
Lyophilized material is typically stored at minus twenty degrees Celsius or lower. Keeping the vial dry and protected from light preserves peptide integrity. Repeated freeze-thaw cycles can cause aggregation or loss of activity. Once dissolved, solutions are generally kept at two to eight degrees Celsius. Stability data for reconstituted solutions vary, and long-term behavior is not fully established. Working aliquots reduce the number of times a stock container is opened.
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.
CJC-1295 is a synthetic peptide designed as a long-acting analogue of growth hormone-releasing hormone (GHRH). Its structure derives from the first 29 amino acids of native GHRH, a fragment often called GRF(1-29). Four substitutions were introduced to slow enzymatic breakdown and extend activity relative to the natural sequence. The compound was developed by ConjuChem as part of a broader effort to improve the pharmacokinetic profile of peptide hormones. It is studied in laboratory and clinical research settings rather than appearing as a naturally occurring substance.
Two related forms circulate in technical discussion under the same family name. The original version carries a drug affinity complex (DAC) that binds covalently to serum albumin after administration, and this linkage substantially extends circulation time. A second form, frequently written as modified GRF(1-29) or CJC-1295 without DAC, lacks that linker and clears much faster. The naming is a frequent source of confusion because the shorthand CJC-1295 can refer to either form depending on the source. Reports sometimes fail to specify which variant was studied.
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=== Substrate specificity === Under normal circumstances, caspases recognize tetra-peptide sequences on their substrates and hydrolyze peptide bonds after aspartic acid residues. Caspase 3 and caspase 7 share similar substrate specificity by recognizing tetra-peptide motif Asp-x-x-Asp. The C-terminal Asp is absolutely required while variations at other three positions can be tolerated. Caspase substrate specificity has been widely used in caspase based inhibitor and drug design.
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Sources: en.wikipedia.org
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=== Alkyl and aryl thiols === Alkyl thiols are the simplest thiols. Methanethiol (CH3SH, methyl mercaptan), ethanethiol (C2H5SH, ethyl mercaptan), propanethiol (C3H7SH), butanethiols (C4H9SH, n-butyl mercaptan and tert-Butyl mercaptan, are common reagents. While these thiols have the characteristic unpleasant odors, some thiols are responsible for the flavor and fragrance of foods, e.g. furan-2-ylmethanethiol. 1-Hexadecanethiol is a lipophilic alkylthiol. Aryl thiols include the parent thiophenol (C6H5SH). Pentachlorobenzenethiol has pesticidal properties.
Sources: en.wikipedia.org
The names are often used interchangeably in casual writing, but they are not strictly identical. Modified GRF(1-29) refers to the unconjugated analogue carrying only the four substitutions. The version sold as CJC-1295 with DAC includes the albumin binding linker and clears much more slowly.
DAC stands for drug affinity complex, a term describing the maleimidopropionic acid linker. This group forms a covalent bond with the cysteine residue on serum albumin after administration. The resulting adduct is what extends the circulating half life from minutes to days.
No. It is entirely synthetic and does not correspond to any known endogenous peptide. The design starts from human growth hormone releasing hormone and introduces deliberate substitutions. Any biological effect comes from mimicking the natural hormone at its receptor.
The mass difference from the linker is large enough for routine detection by mass spectrometry. The unconjugated form gives a single sharp signal at its expected weight. Material that has already reacted with albumin shows a much higher mass and a broadened chromatographic peak.