A practical reference on CJC-1295: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-04-27. Anything still debated is marked as such rather than presented as settled.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C152H252N44O42 | Cited for the form without the drug affinity complex |
| Molecular weight | About 3368 Da | Reported value for modified GRF(1-29) |
| Appearance | White to off-white powder | Lyophilised solid as usually supplied |
| Solubility | Soluble in water and polar solvents | Clarity depends on purity and salt content |
| Typical storage | -20 C or below, dry | Protect from light and repeated warming cycles |
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.
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.
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.
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.
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=== Mechanism of action === Carbetocin works as an oxytocic, antihemorrhagic and uterotonic drug in the peripheral nervous system. The most common causes of postpartum hemorrhage are lack of tone in the uterus from overstretching or the use of an anesthetic. Carbetocin functions as an agonist at peripheral oxytocin receptors, particularly in the myometrium, with lesser affinity for myoepithelial cells. Oxytocin receptors are G protein-coupled and their mechanism of action involves second messengers and the production of inositol phosphates. Carbetocin mimics this mechanism. Binding for carbetocin and other oxytocin agonists has been shown to be nonselective at the extracellular N-terminus and loops E2 and E3. While the oxytocin receptor shows equal affinity for oxytocin and carbetocin, the biological effect of carbetocin is almost 50% that of endogenous or exogenous oxytocin. Carbetocin has a much longer lasting effect than oxytocin, necessitating only a single dose. Carbetocin inhibits endogenous oxytocin release, interrupting the uterine feedback loop with the hypothalamus and decreasing both central and peripheral release of oxytocin. Carbetocin is a biased agonist of the oxytocin receptor. During pregnancy, the synthesis of oxytocin receptors in the uterus greatly increases, reaching a peak during labor and delivery. Consequently, the administration of carbetocin or another oxytocin analog during or immediately following birth will have increased uterotonic and contractile effect.
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=== Patient recorded data === Where the subject is required to record data (e.g. daily symptoms) then a diary is provided for completion. Data management of this data requires a different approach to CRF data as, for example, it is generally not practical to raise data queries. Patient diaries may be developed in either paper or electronic (eDiary) formats. Such eDiaries generally take the form of a handheld device which enables the subject to enter the required data and transmits this data to a centralised server.
==== Sheath-flow interface ==== With the sheath-flow interface, the electrical connection between an electrode and background electrolyte is established when the CE separation liquid is mixed with sheath liquid flowing coaxially in a metal capillary tubing. In most popular commercial CE-ESI-MS interfaces an additional outer tube (three-tube coaxial design) with sheath gas is used, which help to improve electrospray stability and solvent evaporation. But it has been found that flow of sheath gas can cause suction effect near the capillary terminus, which lead to parabolic flow profile and, as a consequence, low separation efficiency. Commonly used sheath liquid is 1:1 mixture of water-methanol (or isopropanol) with 0.1% acetic acid or formic acid. The system is more reliable and has wide selection range of separation electrolyte. However, since flow rates of sheath liquid required for a stable electrospray are usually quite high (1-10 μL/min), here might be some decrease in sensitivity due to dilution of samples with sheath liquid. Sheath liquid can be delivered hydrodynamically (with a syringe pump) or electrokinetically. Electrokinetic method allows one easily operate in nanoelectrospray regime (ESI flow rates at nl/min) and thus to improve sensitivity.There are some new approaches and improvements for sheath-flow interface. To reduce the dead volume and to increase sensitivity extendable sheath-flow CE-ESI-MS interface was created. The outlet end of the separation capillary was treated with hydrofluoric acid to decrease thin of the wall and to taper the tip.
Sources: en.wikipedia.org
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Sources: en.wikipedia.org
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Dopamine receptor blockade Genetically reduced function of dopamine receptor D2 Sympathoadrenal hyperactivity and autonomic dysfunction It has been proposed that blockade of D2-like (D2, D3 and D4) receptors induce massive glutamate release, generating catatonia, neurotoxicity and myotoxicity. Additionally, the blockade of diverse serotonin receptors by atypical antipsychotics and activation of 5-HT1 receptors by some may reduce GABA release and indirectly induce glutamate release, worsening this proposed glutamatergic neurotoxicity. The muscular symptoms are most likely caused by blockade of the dopamine receptor D2, leading to abnormal function of the basal ganglia similar to that seen in Parkinson's disease. In the past, research and clinical studies seemed to corroborate the D2 receptor blockade theory in which antipsychotic drugs were thought to significantly reduce dopamine activity by blocking the D2 receptors associated with this neurotransmitter. The introduction of atypical antipsychotic drugs, with lower affinity to the D2 dopamine receptors, was thought to have reduced the incidence of NMS. However, recent studies suggest that the decrease in mortality may be the result of increased physician awareness and earlier initiation of treatment rather than the action of the drugs themselves. NMS induced by atypical drugs also resembles "classical" NMS (induced by "typical" antipsychotic drugs), further casting doubt on the overall superiority of these drugs.
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Sources: en.wikipedia.org
It is a synthetic peptide analogue of growth hormone-releasing hormone. Four substitutions in its sequence make it more resistant to enzymatic degradation than the natural hormone. In the version carrying a drug affinity complex, the peptide binds albumin and remains in circulation for days.
No regulatory agency has approved CJC-1295 for clinical use. Human trials were conducted in the 2000s, but the development programme was discontinued before any marketing application succeeded. Material sold today is offered as a research chemical, and its purity depends on the supplier.
Sermorelin is an unmodified fragment of growth hormone-releasing hormone and is cleared quickly. CJC-1295 contains substitutions that resist breakdown, and the form with a drug affinity complex persists much longer. Both act at the same receptor but differ substantially in duration of action.
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.