If you have been reading about GHRH analogue 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.
Updated 2025-09-19. Numbers and descriptions here follow the published literature rather than marketing material.
CJC-1295 is a synthetic peptide designed as a long-acting analogue of growth hormone-releasing hormone (GHRH). Its structure derives from the first 29 amino acids of native GHRH, a fragment often called GRF(1-29). Four substitutions were introduced to slow enzymatic breakdown and extend activity relative to the natural sequence. The compound was developed by ConjuChem as part of a broader effort to improve the pharmacokinetic profile of peptide hormones. It is studied in laboratory and clinical research settings rather than appearing as a naturally occurring substance.
Two related forms circulate in technical discussion under the same family name. The original version carries a drug affinity complex (DAC) that binds covalently to serum albumin after administration, and this linkage substantially extends circulation time. A second form, frequently written as modified GRF(1-29) or CJC-1295 without DAC, lacks that linker and clears much faster. The naming is a frequent source of confusion because the shorthand CJC-1295 can refer to either form depending on the source. Reports sometimes fail to specify which variant was studied.
The peptide backbone includes a D-alanine at position two, which resists cleavage by dipeptidyl peptidase IV, and several other substitutions that reduce degradation. Its molecular weight is roughly 3.4 kDa without the linker and about 3.6 kDa with it. The molecule is water soluble and is normally supplied as a lyophilized powder. Precise sequence and mass values depend on which variant is described, so technical documents usually state the exact form being referenced.
Identity and purity are assessed mainly by reversed-phase high-performance liquid chromatography combined with mass spectrometry. The chromatographic separation resolves the target peptide from truncation products and from species carrying oxidised residues, while mass measurement confirms the expected molecular mass. Because the two common variants differ by roughly 280 daltons, a mass determination distinguishes them unambiguously. Purity is often quoted as a percentage of total peak area, although that figure depends on the detection wavelength and the integration method applied.
Reported half-lives differ widely between the two variants and between species. Values for the albumin-binding form are usually expressed in days, while the unconjugated form is measured in minutes to a few hours. Sampling schedules, assay sensitivity, and route of administration all influence the numbers, which limits direct comparison across studies. Whether sustained receptor occupancy produces different downstream effects from pulsatile stimulation remains an open question in the published work. Claims about relative potency should therefore be read alongside the specific study design that produced them.
| Property | Value | Notes |
|---|---|---|
| Molecular weight (no linker) | ~3.37 kDa | Calculated from peptide sequence |
| Molecular weight (with linker) | ~3.65 kDa | Includes albumin-binding moiety |
| Appearance | White to off-white powder | Typically lyophilized |
| Solubility | Soluble in water | Also dissolves in aqueous buffers |
| Common synonyms | Modified GRF(1-29), DAC:GRF | Usage varies by source |
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.
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.
Two principal forms appear in the literature and in research supply. One carries a drug affinity complex, a maleimide-based group that forms a covalent bond with circulating albumin. This linkage slows clearance and produces a long-lasting elevation of peptide levels. The other form lacks that group and is often labeled MOD GRF(1-29). It has a much shorter circulation time. Both variants retain the same core receptor-binding sequence. Reported half-lives differ substantially between the two.
At the pituitary, the peptide binds the growth hormone-releasing hormone receptor on somatotroph cells. Receptor activation raises intracellular cyclic AMP and triggers release of stored growth hormone. Somatostatin and other hypothalamic signals modulate this response. Negative feedback from insulin-like growth factor 1 also influences output. The same regulatory architecture operates with the native hormone. Whether the synthetic analog alters feedback dynamics over repeated exposure remains an open question. Most published receptor work uses cell models rather than intact human systems.
CJC-1295 acts at the growth hormone-releasing hormone receptor, a G-protein-coupled receptor found on somatotroph cells in the anterior pituitary. Binding triggers a rise in cyclic AMP and calcium entry, which promotes release of stored growth hormone. Because the peptide mimics the body's own releasing hormone, it amplifies existing secretory pulses rather than driving continuous output. The size of the response therefore depends partly on the subject's own hormonal rhythm and feedback state.
The attached maleimide group explains the unusual duration of the DAC version. After injection it reacts with the thiol of cysteine-34 on serum albumin, forming a stable covalent bond. The resulting conjugate is too large for rapid kidney filtration and is shielded from many peptidases. Reported half-lives for this form reach several days, whereas the version without the group is cleared in roughly half an hour. That gap is the main pharmacological difference between the two.
== Bibliography == Danish-language bibliography Rasmussen, Carsten Porskrog (2019). Hertugdømmet (in Danish). Aarhus Universitetsforlag. ISBN 978-87-7184-761-1. Gram-Andersen, Jesper (2020). De kongelige hertugdømmer: skydebrødre i Det Kongelige Kjøbenhavnske Skydeselskab og Danske Broderskab med relation til Slesvig og Holsten (in Danish). Kle-art. ISBN 978-87-92750-32-7. Jensen, N. P. (23 January 2019). Den første slesvigske krig 1848-50 (in Danish). Lindhardt og Ringhof. ISBN 978-87-26-10014-3. Buk-Swienty, Tom (2009). Slagtebænk Dybbøl: 18. april 1864 : historien om et slag (in Danish). Gyldendal A/S. ISBN 978-87-02-07756-8.< Frandsen, Steen Bo (2008). Holsten i helstaten: hertugdømmet inden for og uden for det danske monarki i første halvdel af 1800-tallet (in Danish). Museum Tusculanums Forlag, Københavns Universitet. ISBN 978-87-635-0754-7. Korsgaard, Ove (2024). Nationalstatens fødselsveer: Grundtvig, krig og geopolitik. Aarhus: Aarhus University Press. ISBN 978-87-7597-394-1. German language bibliography Wenners, Peter (2019). Schleswig-Holstein und Dänemark: Geschichte im Spiegel der Literatur (in German). Boyens. ISBN 978-3-8042-1513-9. Jung, Frank (1 September 2014). 1864 - Der Krieg um Schleswig-Holstein (in German). Ellert & Richter Verlag. ISBN 978-3-8319-1016-8. English language bibliography Svendsen, Nick B. (11 September 2018). Medieval wars in the Duchy of Schleswig 1410 to 1432: and the quest for the Nordic Countries. Books on Demand. ISBN 978-87-430-0687-9. Dicey, Edward; Lowe, Charles (9 June 2016).
=== International guidelines === The World Cancer Research Fund recommends limiting red meat to no more than three servings per week. The European Association for the Study of Diabetes recommends that diabetics minimise the consumption of red meat.
MR-2096 is an opioid analgesic drug related to oxymorphone. It has an unusual chiral tetrahydrofuran-2-ylmethyl substitution on the nitrogen which determines the character of effects, with the (R) enantiomer MR-2096 being an opioid agonist, while the (S) enantiomer MR-2097 has similarly potent opioid antagonist effects. This mix of activities has made these two enantiomers useful for characterising the binding site of the mu opioid receptor.
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Sources: en.wikipedia.org
Walton and Torbjørn Sikkeland, used the new heavy-ion linear accelerator (HILAC) to bombard a curium target (95% 244Cm and 5% 246Cm) with 13C and 12C ions. They were unable to confirm the 8.5 MeV activity claimed by the Swedes but were instead able to detect decays from 250Fm, supposedly the daughter of 254No (produced from the 246Cm), which had an apparent half-life of ~3 s. Probably this assignment was also wrong, as later 1963 Dubna work showed that the half-life of 254No is significantly longer (about 50 s). It is more likely that the observed alpha decays did not come from element 102, but rather from 250mFm. In 1959, the Swedish team attempted to explain the Berkeley team's inability to detect element 102 in 1958, maintaining that they did discover it. However, later work has shown that no nobelium isotopes lighter than 259No (no heavier isotopes could have been produced in the Swedish experiments) with a half-life over 3 minutes exist, and that the Swedish team's results are most likely from 225Th, which has a half-life of 8 minutes and quickly undergoes triple alpha decay to 213Po, which has a decay energy of 8.53612 MeV. This hypothesis is lent weight by the fact that 225Th can easily be produced in the reaction used and would not be separated out by the chemical methods used. Later work on nobelium also showed that the divalent state is more stable than the trivalent one and hence that the samples emitting the alpha particles could not have contained nobelium, as the divalent nobelium would not have eluted with the other trivalent actinides.
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Sources: en.wikipedia.org
No. It is a synthetic analogue modeled on the first 29 residues of human GHRH. The substitutions and any linker are laboratory modifications rather than features of the endogenous peptide.
Early development used the albumin-binding form, and a shorter variant was later discussed under the same label. Because the two differ in half-life and handling, ambiguity arises whenever a source omits the variant designation.
The compound derives from that fragment but is not identical to it. The parent fragment lacks the stabilizing substitutions, so its degradation rate and duration of action differ noticeably.
Chromatography reports how much material elutes as a single peak but does not confirm what that material is. Mass spectrometry supplies the molecular mass, which is characteristic of a given sequence and its modifications. Together the two methods support both a purity figure and an identity claim.