Compound monograph
CJC-1295
CJC-1295 designates a tetrasubstituted analog of human growth hormone-releasing factor residues 1 to 29, reported to act at the GRF receptor on the anterior pituitary.
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Identity & nomenclature
CJC-1295 designates a tetrasubstituted analog of human growth hormone-releasing factor residues 1 to 29, reported to act at the GRF receptor on the anterior pituitary.
The name CJC-1295 is used in the literature and in commerce for two distinct species. The compound identified in the original report is a tetrasubstituted form of hGRF(1-29) bearing an N-epsilon-3-maleimidopropionamide derivative of lysine at the C-terminus; that maleimido group is the drug affinity complex, and it bioconjugates in vivo to the free thiol at Cys34 of serum albumin. Material sold as CJC-1295 without DAC lacks that linker and does not form the albumin conjugate, and is the species this record describes; it is the CJC-1295 component of the catalog's CJC-1295 / ipamorelin blend, while the catalog's CJC-1295 With DAC listing is the other species. PubChem CID 56841945 encodes the non-DAC 29-mer with D-Ala2 and Arg29-amide (C152H252N44O42; 3367.95 Da), whereas CID 91971820 encodes the DAC species (C165H269N47O46; 3647.2 Da; CAS 446262-90-4; UNII 62RC32V9N7); CID 91976842 omits stereochemistry. PubChem CID 91971820, CAS 446262-90-4 and GSRS UNII 62RC32V9N7 identify the DAC form and are excluded from this non-DAC record. No CAS or UNII is published for the non-DAC species because none could be verified against a primary registry. Identity should be established against the intended species, and a supplier certificate quoting 3647.2 Da is describing the other molecule.
Declared aliases and development codes: CJC 1295.
02
Molecular properties
| Molecular formula | C152H252N44O42 |
|---|---|
| Molecular mass | 3367.95 Da |
| PubChem CID | 56841945 |
| Three-letter sequence | Tyr–D-Ala–Asp–Ala–Ile–Phe–Thr–Gln–Ser–Tyr–Arg–Lys–Val–Leu–Ala–Gln–Leu–Ser–Ala–Arg–Lys–Leu–Leu–Gln–Asp–Ile–Leu–Ser–Arg |
| Terminal groups | Free N-terminus; C-terminal amide at Arg29 |
Twenty-nine residues, the tetrasubstituted hGRF(1-29) analog without the drug affinity complex. Against unmodified GRF(1-29), recorded on the sermorelin entry as YADAIFTNSYRKVLGQLSARKLLQDIMSR, the four changes are D-alanine at position 2, glutamine for asparagine at position 8, alanine for glycine at position 15, and leucine for methionine at position 27. No one-letter string is published here: one-letter symbols denote L residues unless marked, so writing position 2 as A would state the L-alanine of the parent fragment. The D-configuration has the same elemental composition, so the three-letter chain still derives the recorded formula and mass. The substitution at position 27 removes the only sulfur-containing residue of the parent fragment, which is why this record has no sulfur while sermorelin does.
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Structural characteristics
The original report describes synthesis of three maleimido derivatives of hGRF(1-29) and their ex vivo bioconjugation to human serum albumin, with all three conjugates showing enhanced in vitro stability against dipeptidyl peptidase IV; the compound selected from that series is the DAC-bearing form. That report characterises the conjugate, not the peptide described here. What this record shares with it is the tetrasubstituted hGRF(1-29) backbone; the maleimidopropionamide lysine that made the conjugation possible is exactly what the non-DAC species lacks.
Terminal features: Free N-terminus, C-terminal amide at Arg29.
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Molecular targets & mechanisms
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Analytical considerations
Because the DAC and non-DAC species differ by an appended lysine and its maleimidopropionamide group, mass-based identity methods distinguish them directly and unambiguously: 3367.95 Da against 3647.2 Da, a 279.3 Da gap no instrument would miss. The recorded formula contains no sulfur, because the position-27 methionine of the parent fragment is substituted to leucine; a sulfur signal in a sample of this species is therefore a finding, not noise. A conjugated sample additionally carries albumin, which alters apparent mass by roughly the mass of serum albumin and requires a method that resolves the conjugate rather than the free peptide.
Disagreements and mix-ups
Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.
Often mixed up · Registry identifier
CJC-1295 with and without the drug affinity complex
What the studies reported
Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.
Cell and tissue studies
Albumin-conjugated hGRF derivatives and cultured rat anterior pituitary cells
Jetté et al. reported increased stability against dipeptidylpeptidase-IV and GH-secretion activity for albumin-conjugated derivatives, including CJC-1295, in cultured rat anterior pituitary cells.
Reference [1]
Animal studies
Male Sprague Dawley rats
Jetté et al. detected CJC-1295 in plasma beyond 72 h in male Sprague Dawley rats.
Reference [1]Rat plasma in Western blot analysis
Jetté et al. detected CJC-1295 immunoreactivity at the serum-albumin band in rat plasma, appearing after 15 min and remaining in circulation beyond 24 h.
Reference [1]GHRH-knockout mice
Alba et al. reported increased total pituitary RNA and GH mRNA in GHRH-knockout mice receiving CJC-1295.
Reference [2]
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Verified bibliography
Cited studies by type
The 3 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.
A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.
Reference 1
Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog.Jetté L, Léger R, Thibaudeau K, Benquet C, Robitaille M, Pellerin I, Paradis V, van Wyk P, Pham K, Bridon DP
Endocrinology · 2005-04-07 · Journal Article
currentReference 2
Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse.Alba M, Fintini D, Sagazio A, Lawrence B, Castaigne JP, Frohman LA, Salvatori R
American journal of physiology. Endocrinology and metabolism · 2006-07-05 · Journal Article
currentReference 3
Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults.Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA
The Journal of clinical endocrinology and metabolism · 2005-12-13 · Journal Article
current
Study models of these references
What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.
| Reference | Study models |
|---|---|
| Jetté L et al. 2005 | Study models reported: in vitro; animal (rat) · from the abstract |
| Alba M et al. 2006 | Study models reported: animal (mouse) · from the abstract |
| Teichman SL et al. 2005 | Study models reported: human participants (interventional) · from the abstract |
Compare
Record history
Published 2026-09-04.
- : Identity and nomenclature
- : Sequence and structure
- : Sequence and structure
- : Identity and nomenclature
- : Sequence and structure
- : Identity and nomenclature, Sequence and structure, Analytical notes
Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.
Cite this record: Purely Peptides Research Library. CJC-1295. Published 2026-09-04; updated 2026-10-21. https://purelypeptides.org/research/compounds/cjc-1295/
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Methodology & citation verification
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