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CJC-1295 vs Sermorelin

These records distinguish the substituted non-DAC backbone recorded as CJC-1295 from sermorelin’s GRF(1-29) sequence. The cited CJC report concerns DAC-bearing conjugates; its species must not be conflated with this non-DAC record.

Published: 2026-10-03Library record comparison: 2026-10-03

01

Identity side by side

Recorded molecular identities of CJC-1295 and Sermorelin
Recorded fieldCJC-1295Sermorelin
Canonical nameCJC-1295Sermorelin
AliasesCJC 1295GRF(1-29); Sermorelina; Sermorelinum
Development codesnot recordednot recorded
CASnot recorded86168-78-7
UNIInot recorded89243S03TE
PubChem CID9197684216132413
Molecular formulaC152H252N44O42C149H246N44O42S
Molecular weight (Da)3367.953357.9
Sequence length (residues)2929
Terminal modificationsC-terminal amide at Arg29C-terminal amide at Arg29
Structural modificationsnot recordednot recorded

CJC-1295: nomenclature notes

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 and the species sold as product 1023. The two are separated by 279.3 Da: the non-DAC peptide is C152H252N44O42 at 3367.95 Da, PubChem CID 91976842; the DAC form is C165H269N47O46 at 3647.2 Da, PubChem CID 91971820, CAS 446262-90-4, UNII 62RC32V9N7. Those registry numbers belong to the DAC form and are deliberately not carried here. 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.

Sermorelin: nomenclature notes

Sermorelin corresponds to residues 1 to 29 of human growth hormone-releasing factor, the fragment commonly written GRF(1-29). Both CJC-1295 and tesamorelin, also in this library, are modified derivatives of this same fragment: CJC-1295 through a C-terminal maleimidopropionamide lysine substitution enabling albumin conjugation, and tesamorelin through a separate structural modification.

02

Residue sequence comparison

Positions are numbered from each stored sequence’s first residue. Highlighted cells differ or extend beyond the other chain; a dash indicates no aligned residue. One-letter notation does not encode terminal groups or stereochemistry. Read the recorded notes below.

Aligned one-letter residue sequences
CJC-12951Y2A3D4A5I6F7T8Q9S10Y11R12K13V14L15A16Q17L18S19A20R21K22L23L24Q25D26I27L28S29R
Sermorelin1Y2A3D4A5I6F7T8N9S10Y11R12K13V14L15G16Q17L18S19A20R21K22L23L24Q25D26I27M28S29R

Differences in text

  • CJC-1295: residue 8 = Q; Sermorelin: residue 8 = N.
  • CJC-1295: residue 15 = A; Sermorelin: residue 15 = G.
  • CJC-1295: residue 27 = L; Sermorelin: residue 27 = M.

CJC-1295

Terminal modifications
C-terminal amide at Arg29
Structural modifications
not recorded
Stored three-letter notation
Tyr · 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
Sequence notes
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. Position 2 is the D-enantiomer; oneLetter records it as A because the derivation model does not represent stereochemistry, and the D-configuration is elementally identical to L-alanine, so it is recorded here instead of being lost. 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.

Sermorelin

Terminal modifications
C-terminal amide at Arg29
Structural modifications
not recorded
Stored three-letter notation
Tyr · Ala · Asp · Ala · Ile · Phe · Thr · Asn · Ser · Tyr · Arg · Lys · Val · Leu · Gly · Gln · Leu · Ser · Ala · Arg · Lys · Leu · Leu · Gln · Asp · Ile · Met · Ser · Arg
Sequence notes
The N-terminal 29 residues of human growth hormone-releasing hormone, carried as a C-terminal amide. The recorded molecular formula and mass are the values this sequence derives with that amide applied; without it the derivation gives the free acid and does not match.

03

Recorded mechanisms

These lists show the links recorded in each monograph. An unlisted link does not establish its absence from the molecule’s biology.

Shared recorded links

Recorded only for CJC-1295

not recorded

Recorded only for Sermorelin

not recorded

04

Recorded compound classes

Shared recorded links

Recorded only for CJC-1295

not recorded

Recorded only for Sermorelin

not recorded

05

References for the relationship

  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

    current

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Read the full monographs