CJC-1295 comes up often in conversation and rarely with the context attached. Here we lay out the basics in order, then work through the practical considerations.
Last reviewed on 2026-08-01. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
Stability depends heavily on physical state. A lyophilized powder kept dry, desiccated, and shielded from light typically holds its integrity for months to years at minus twenty degrees Celsius, and longer at minus eighty. Once dissolved, the peptide becomes far more vulnerable, since peptide bond hydrolysis, oxidation of susceptible residues, and aggregation all proceed faster in solution. Buffers near neutral pH are generally gentler than strongly acidic or alkaline conditions. Repeated freeze-thaw cycles and exposure to air-liquid interfaces during vigorous mixing cause losses that are easy to overlook.
Verification matters because research peptides vary widely in quality. A certificate of analysis is only as reliable as the method behind it, and a single chromatographic trace reveals little about counter-ions, residual solvents, or water content. Independent laboratories commonly pair mass confirmation with chromatographic purity and, where relevant, quantify water along with acetate or trifluoroacetate content. Reported purity figures are not standardized across suppliers, so a stated value such as ninety-eight percent is not directly comparable unless the analytical method, column, and detection wavelength accompany it.
Characterization of this peptide relies on a small set of routine techniques. Reversed-phase high-performance liquid chromatography separates the target from truncated or oxidized by-products and yields a purity estimate when paired with ultraviolet detection near 214 nanometers. Mass spectrometry, either electrospray coupled to liquid chromatography or matrix-assisted laser desorption, confirms that the observed mass matches the value calculated for the expected sequence. Amino acid analysis, and enzymatic digestion followed by fragment mapping, are used when the sequence itself rather than the mass requires verification.
| Property | Value | Notes |
|---|---|---|
| Class | Synthetic peptide | GHRH receptor agonist |
| Sequence length | 29 amino acids | Derived from human GHRH |
| Molecular weight | About 3368 Da without linker | Albumin-binding form is heavier |
| Appearance | White to off-white lyophilized powder | Common form for research reference material |
| Typical storage | -20 °C or below, desiccated | Protect powder from light and moisture |
CJC-1295 is a synthetic peptide built as a long-acting analogue of growth hormone-releasing hormone. Its backbone matches the first twenty-nine residues of the natural human hormone, with four amino acid substitutions added to slow enzymatic breakdown. A reactive maleimide group, commonly termed the drug affinity complex, allows the peptide to attach to circulating albumin after administration. That albumin attachment keeps the molecule in the bloodstream for an extended period instead of being cleared within minutes.
The compound emerged from work at a Canadian biotechnology firm in the early 2000s. Early human studies examined its effect on growth hormone and insulin-like growth factor 1 in healthy volunteers and in people with HIV-associated fat redistribution. Reports described sustained increases in both markers after a single injection. Development did not advance to regulatory approval, and the clinical programme was later discontinued. The molecule is now encountered mainly as a research chemical rather than a marketed medicine.
Two forms circulate in research settings and are frequently confused. One carries the drug affinity complex and is often written as CJC-1295 with DAC; the other lacks that group and is usually called modified GRF(1-29). The two share the same core sequence but differ sharply in how long they persist in blood. Products labelled only as CJC-1295 normally refer to the version carrying the complex. Documentation that omits the distinction leaves the intended molecule ambiguous.
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.
Four amino acid substitutions separate the modified backbone from the parent GRF(1-29) sequence. These changes reduce recognition by dipeptidyl peptidase IV and related proteases, extending the interval before degradation. Development work in this area sought longer-acting GHRH analogs for endocrine investigation. Published descriptions treat the substitution set as a defining property of the core sequence, while the albumin-binding linker is described separately as an optional addition to that same backbone.
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.
== Further reading == Gustavo V. Barbosa-Canovas, Liliana Alamilla-Beltran, Efren Parada-Arias, Jorge Welti-Chanes (2015) Water Stress in Biological, Chemical, Pharmaceutical and Food Systems. New York, NY : Springer New York : Imprint: Springer. ISBN 978-1-4939-2578-0 Jamuna Aswathanarayn & Rai, V. Ravishankar (2015). Microbial Food Safety and Preservation Techniques. Boca Raton : CRC Press Taylor & Francis Group. ISBN 9781138033801
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The International Mass Spectrometry Foundation (IMSF) is a non-profit scientific organization in the field of mass spectrometry. It operates the International Mass Spectrometry Society, which consists of 37 member societies and sponsors the International Mass Spectrometry Conference that is held once every two years.
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Sources: en.wikipedia.org
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Additionally, CAM providers are concerned by the closure of other CAM laboratories under CLIA, and have sought to avoid detection. Some CAM providers and laboratory personnel have not had exposure to laboratory curriculum and are unaware of CLIA requirements. CLIA is largely reliant on laboratories to self-identify themselves for enrollment. Providers of CAM laboratories have opposed CLIA oversight and suggested they be regulated by their peers or by a CAM-specific division. CAM providers have stated that they should be exempt from CLIA since CAM laboratories do not participate in health insurance. Others claim that they are exempt from CLIA because the tests are performed solely for research purposes and not used in patient care and treatment decisions. Several pathologists have stated that CAM testing falls within the scope of their medical license and should not be regulated under CLIA. CLIA provisions are geared towards CLIA-certified laboratories, but not for those that have not enrolled. When a CAM laboratory is found to be operating without a CLIA certificate, they are sent a cease and desist letter to stop testing until the laboratory is CLIA certified. There are no administrative remedies available to CMS when a laboratory refuses to enroll in CLIA and refuses to cease testing. CMS cannot impose monetary or other administrative penalties on laboratories that defy the law, but can only refer cases to other Federal or State agencies.
=== Simultaneous cyclization/resin release === Small C-terminal cyclic moieties like γ-, δ-, and ε-lactams can be introduced in peptides synthesized on base-labile linkers by deprotecting the C-terminal amino acid bearing an amine on its side-chain and letting it cyclize, thereby releasing the peptide from the resin in the process.
Sources: en.wikipedia.org
Natural GHRH is degraded quickly by dipeptidyl peptidase-4 and related enzymes, giving it a half-life measured in minutes. CJC-1295 carries substitutions that slow that breakdown, so it stays intact longer. Both act at the same pituitary receptor and produce the same class of signal.
The label was first attached to the albumin-binding form during early development work. A shorter analog without the linker later became known by the same name in informal use. Published papers normally state which version was studied, so the methods section resolves the ambiguity.
It is a synthetic peptide rather than a steroid, and it does not occur naturally in the body. Its sequence is derived from a hypothalamic hormone called growth hormone-releasing hormone. It works as a receptor agonist rather than as a replacement for that hormone.
Mass spectrometry establishes whether the observed molecular weight matches the calculated sequence mass. Chromatographic retention and fragment mapping add further confidence about sequence and composition. A single technique alone is rarely treated as sufficient evidence of identity.