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Metabolic researchComponent research

CJC-1295/Ipamorelin Blend

A named pairing of a growth hormone releasing factor analogue with a pentapeptide secretagogue, where the CJC name alone does not establish whether the albumin-reactive modification is present. Every reference here belongs to one constituent or the other. No study of the mixture itself is cited.

For in-vitro research only.Reviewed 2026-09-20

Key findings

  • The CJC constituent is described as a tetrasubstituted form of the 1-29 fragment carrying an N-epsilon-3-maleimidopropionamide derivative of lysine at the C terminus, the group that conjugates to serum albumin. [1]
  • Detection work lists CJC-1295 and CJC-1295 with drug affinity complex as separate target analytes, so the two forms are distinguished analytically and not by name. [2]
  • The second constituent is the pentapeptide Aib-His-D-2-Nal-D-Phe-Lys-NH2, which released growth hormone from primary rat pituitary cells with an EC50 of 1.3 nmol/l through a GHRP-like receptor. [3]
  • Once conjugated the CJC construct behaves as a macromolecule of undefined mass, which is why the cited screens used immuno-polymerase chain reaction or immuno-affinity capture rather than top-down mass spectrometry. [4]
CJC-1295 with DAC profileIpamorelin profile

Identity and structure

Catalog name
A two-component listing whose name gives neither constituent amount
Composition
Constituent amounts come from the lot documentation; this profile does not assign them, and a combined fill mass does not give the amount of either peptide
Drug affinity complex status
The blend name does not by itself establish whether the albumin-reactive modification is present, because detection work lists CJC-1295 and CJC-1295 with drug affinity complex as distinct analytes [2]
First constituent
A tetrasubstituted form of human growth hormone releasing factor 1-29 bearing a maleimide group at the C terminus [1]
Second constituent
The pentapeptide Aib-His-D-2-Nal-D-Phe-Lys-NH2 [3]
Form as supplied
Sterile lyophilized powder

Mechanism as studied

The maleimide group reacts with the free thiol of Cys34 on serum albumin. Three maleimido derivatives of the 1-29 fragment conjugated to human serum albumin ex vivo were all resistant to dipeptidylpeptidase IV in vitro and all active on cultured rat anterior pituitary cells. [1]

The pentapeptide reaches growth hormone release through a different receptor. Antagonist profiling in primary rat pituitary cells placed its action at a GHRP-like receptor rather than at the growth hormone releasing hormone receptor. [3]

Research findings

In vitro
System
Three maleimido derivatives of the 1-29 fragment conjugated ex vivo to human serum albumin and assayed on cultured rat anterior pituitary cells; the study material is that constituent alone
Measured
Stability against dipeptidylpeptidase IV and growth hormone secretion from the cultured cells
Reported
All three albumin conjugates showed enhanced in-vitro stability against dipeptidylpeptidase IV and were bioactive in the growth hormone secretion assay. [1]
In vitro
System
Primary rat pituitary cells with GHRP and growth hormone releasing hormone antagonists; the study material is the pentapeptide alone
Measured
Growth hormone release potency and efficacy relative to GHRP-6, receptor pathway by antagonist blockade
Reported
EC50 was 1.3 plus or minus 0.4 nmol/l with an efficacy of 85 plus or minus 5 percent of the GHRP-6 maximum, and antagonist profiling indicated a GHRP-like receptor. [3]
Analytical
System
Equine plasma with monoclonal antibodies raised against the CJC peptide, read by immuno-polymerase chain reaction; the pentapeptide is not among the analytes
Measured
Limit of detection for the peptide protein conjugate and the screening threshold imposed by endogenous growth hormone releasing hormone
Reported
The conjugate was detected down to 0.8 pg/mL, and endogenous equine growth hormone releasing hormone required a screening threshold of 50 pg/mL. [4]
Order CJC-1295/Ipamorelin Blend with the certificate for the lot that ships

Handling for in-vitro work

Storage
Lyophilized material kept at minus 20 degrees C, dark and dry; reconstituted aliquots kept cold and used promptly

Open questions

  • Whether the supplied CJC constituent carries the albumin-reactive modification is an analytical identity question; the cited methods separate the two forms but no cited study reports a result for catalog material.
  • No cited study characterises this mixture, so constituent amounts, stability and any interaction of the two peptides in solution remain documentation questions.

Lot records

Check the record for the exact material you order. A published paper and a batch certificate answer different questions.

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References

  1. Jetté L, Léger R, Thibaudeau K, et al. 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. Endocrinology. 2005.

    PubMed 15817669 · doi:10.1210/en.2004-1286

  2. Memdouh S, Gavrilović I, Ng K, et al. Advances in the detection of growth hormone releasing hormone synthetic analogs. Drug testing and analysis. 2021.

    PubMed 34665524 · doi:10.1002/dta.3183

  3. Raun K, Hansen BS, Johansen NL, et al. Ipamorelin, the first selective growth hormone secretagogue. European journal of endocrinology. 1998.

    PubMed 9849822 · doi:10.1530/eje.0.1390552

  4. Timms M, Ganio K, Forbes G, et al. An immuno polymerase chain reaction screen for the detection of CJC-1295 and other growth-hormone-releasing hormone analogs in equine plasma. Drug testing and analysis. 2019.

    PubMed 30489688 · doi:10.1002/dta.2554

Publication records fetched from PubMed on 2026-09-20. Profile text reviewed 2026-09-20.