CJC-1295 raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
Reviewed 2026-07-03. Anything still debated is marked as such rather than presented as settled.
Two forms circulate under the CJC-1295 name, and they differ by a single appended group. The version without a drug affinity complex carries four substitutions along the peptide chain, including a D-alanine near the amino terminus and replacements at three other positions. These changes block the enzyme dipeptidyl peptidase IV and remove a methionine residue that is prone to oxidation. The modified fragment is frequently labeled MOD GRF 1-29. Naming conventions are inconsistent across informal sources, which is a common source of confusion.
The second form adds a maleimide-bearing linker to the lysine at the carboxyl end. This group reacts with cysteine-34 on circulating serum albumin, forming a covalent bond that keeps the peptide in the bloodstream for far longer. ConjuChem developed the molecule as a way to extend the action of a peptide without frequent administration. The albumin attachment is the defining structural feature of the drug affinity complex version. Whether continuous exposure produces effects distinct from shorter pulses remains an unresolved research question.
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.
| 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 |
CJC-1295 is a synthetic analogue of growth hormone-releasing hormone, built on the 29-amino-acid GHRH(1-29) fragment. Four substitutions distinguish it from the natural sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27. These changes reduce enzymatic cleavage and extend the peptide's persistence in circulation. The compound is discussed in two forms, one carrying a drug affinity complex and one without it.
The drug affinity complex is a maleimidopropionic acid group attached to a lysine side chain. It reacts with the free thiol of cysteine-34 on circulating albumin, forming a covalent bond. This conjugation keeps the peptide in the bloodstream and shields it from rapid renal filtration and proteolysis. Reported circulation half-lives for the albumin-bound form fall in the range of roughly six to nine days in early human studies.
Binding to GHRH receptors on pituitary somatotroph cells triggers cyclic AMP signaling and stimulates growth hormone synthesis and release. Because the peptide acts upstream of the pituitary, effects are mediated through endogenous growth hormone rather than direct receptor activation in peripheral tissues. Increases in insulin-like growth factor 1 are generally described as a downstream consequence. Most published human exposure data come from small early-stage studies, and the clinical significance of the pharmacokinetic profile remains incompletely characterized.
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.
== See also == Substituted methoxyphenethylamine Scaline § Related compounds Dimethoxyphenethylamine 3-Methoxytyramine Mescaline 3-Methoxy-4-ethoxyphenethylamine (MEPEA; 3-desmethoxyescaline) 3-Methoxy-4-allyloxyphenethylamine (MAPEA; 3-desmethoxyallylescaline) Pachycereus pringlei § Constituents and effects
The Danish currency is the Danish krone, subdivided into 100 øre. The krone and øre were introduced in 1875, replacing the former rigsdaler and skilling. Denmark has a very long tradition of maintaining a fixed exchange-rate system, dating back to the period of the gold standard during the time of the Scandinavian Monetary Union from 1873 to 1914. After the breakdown of the international Bretton Woods system in 1971, Denmark devalued the krone repeatedly during the 1970s and the start of the 1980s, effectively maintaining a policy of "fixed, but adjustable" exchange rates. Rising inflation led to Denmark declaring a more consistent fixed exchange-rate policy in 1982. At first, the krone was pegged to the European Currency Unit or ECU, from 1987 to the Deutsche Mark, and from 1999 to the euro. Although eligible, Denmark chose not to join the European Monetary Union when it was founded. In 2000, the Danish government advocated Danish EMU membership and called a referendum to settle the issue. With a turn-out of 87.6%, 53% of the voters rejected Danish membership. Occasionally, the question of calling another referendum on the issue has been discussed, but since the 2008 financial crisis, opinion polls have shown a clear majority against Denmark joining the EMU, and the question is not high on the political agenda presently. Maintenance of the fixed exchange rate is the responsibility of Danmarks Nationalbank, the Danish central bank.
== Additives == Mobile phase pH and electrostatic interactions, as well as analyte polarity, are regulated by the addition of ionic additives. These additives improve separation efficiency, including more symmetric peaks, less peak tailing, and better recovery from the stationary phase. Ammonium acetate and ammonium formate are commonly used, as they have good solubility in high organic. When considering additive addition, compatibility with detectors is important to consider. HILIC is often used with a mass spectrometry (MS), which cannot handle non-volatile salts like sodium perchlorate, which may suppress ion signal in the instrument, though it may increase mobile phase polarity and assist with elution in HILIC.
Sources: en.wikipedia.org
== Memberships == Burnham has held senior positions and leadership roles in several professional organizations, including the American Society for Microbiology, Clinical and Laboratory Standards Institute, the American Society for Microbiology, and the Academy of Clinical Laboratory Physicians and Scientists.
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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.
The two share the same 29-amino-acid backbone. CJC-1295 carries an additional albumin-binding moiety that markedly extends its residence time in circulation, while the form without that moiety clears faster. Literature sometimes applies the name loosely to either variant.