If you have been reading about CJC-1295 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.
Last reviewed on 2025-11-28. Where a claim depends on a specific study, the study is described rather than over-claimed.
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 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.
Pharmacokinetic behaviour differs sharply between the two forms. The DAC-bearing peptide shows an extended circulation time measured in days, whereas the version without the complex is cleared within roughly half an hour. This gap shapes how researchers design dosing schedules in animal models. Whether the prolonged presence of the DAC form produces effects meaningfully different from the short-acting variant remains an open question, since comparative human data are scarce.
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.
| 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 |
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.
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.
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.
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.
=== Protein fold === A protein fold refers to the general protein architecture, like a helix bundle, β-barrel, Rossmann fold or different "folds" provided in the Structural Classification of Proteins database. A related concept is protein topology.
=== Knowledge-based === A typical data-mining-based prediction uses support-vector machines, decision trees, or neural networks. This method is usually very successful for calculating log P values when used with compounds that have similar chemical structures and known log P values. Molecule mining approaches apply a similarity-matrix-based prediction or an automatic fragmentation scheme into molecular substructures. Furthermore, there exist also approaches using maximum common subgraph searches or molecule kernels.
is different for different electrolytes, even at the same ionic strength. There does not need to be any chemical interaction between the species in equilibrium and the background electrolyte, but such interactions might occur in particular cases. For example, phosphates form weak complexes with alkali metals, so, when determining stability constants involving phosphates, such as ATP, the background electrolyte used will be, for example, a tetralkylammonium salt. Another example involves iron(III), which forms weak complexes with halide and other anions, but not with perchlorate ions. When published constants refer to an ionic strength other than the one required for a particular application, they may be adjusted by means of specific ion theory (SIT) and other theories.
°C), which aligns well with modeled results of methane formation temperature and yield. However, some thermogenic methane samples have clumped-isotope temperatures that are unrealistically high. Possible explanations for exceedingly high clumped isotope temperatures include natural gas migration after formation, mixing effect, and kinetic isotope effect of secondary cracking.
Sources: en.wikipedia.org
Durand sold the patent to Bryan Donkin, who spent two years perfecting the method. Canned food subsequently began to be issued to the Royal Navy. The reason for lack of spoilage was unknown at the time, since it would be until the 1860s before Louis Pasteur demonstrated the role of microbes in food spoilage and developed pasteurization. The Crimean War saw issues with supplying soldiers in battle. In the British Army, rations were regularly halved, and many soldiers developed scurvy, to the point that the hospital in Scutari received more soldiers for scurvy than battle wounds. During the American Civil War, the food and rations of the Union Army and the Confederate States Army were meant to be mostly the same—meat, cornmeal, vegetables, vinegar, molasses, and hardtack—but supply issues plagued the Confederates as the war continued, forcing them to live off the land. The standard Union Army ration was roughly three-quarters pound (340 g) of meat, one pound (450 g) of flour or cornmeal, vegetables, vinegar, and molasses. To ensure that food lasted longer, rations often came in the form of hardtack biscuits, salted meat, and dehydrated vegetables. During campaigns, particularly as Union troops entered the south, seasonal fruits and vegetables were pillaged from farms and orchards. Both the Union and Confederate armies relied on lakes and streams for their water.
== Practical applications == With the human genome sequenced, the next step is the verification and functional annotation of all predicted genes and their protein products. Shotgun proteomics can be used for functional classification or comparative analysis of these protein products. It can be used in projects ranging from large-scale whole proteome to focusing on a single protein family. It can be done in research labs or commercially.
== Similarities with TCA cycle == The glyoxylate cycle uses five of the eight enzymes associated with the tricarboxylic acid cycle: citrate synthase, aconitase, succinate dehydrogenase, fumarase, and malate dehydrogenase. The two cycles differ in that in the glyoxylate cycle, isocitrate is converted into glyoxylate and succinate by isocitrate lyase (ICL) instead of into α-ketoglutarate. This bypasses the decarboxylation steps that take place in the citric acid cycle (TCA cycle), allowing simple carbon compounds to be used in the later synthesis of macromolecules, including glucose. Glyoxylate is subsequently combined with acetyl-CoA to produce malate, catalyzed by malate synthase. Malate is also formed in parallel from succinate by the action of succinate dehydrogenase and fumarase. The difference between the two cycles can be seen through their net equations. In the citric acid cycle, two carbons that are part of the acetyl-CoA are lost as carbon dioxide, which results in net carbon loss. Unlike the citric acid cycle, the glyoxylate cycle bypasses the two decarboxylations. This allows the glyoxylate cycle the net synthesis of glucose from acetyl-CoA. The net equation of the glyoxylate cycle is: 2Acetyl-CoA + NAD+ + 2H2O → Succinate + 2CoA + NADH + H+.
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.
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.