Everything below concerns GHRH analog. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2026-02-11. Where a claim depends on a specific study, the study is described rather than over-claimed.
CJC-1295 is a synthetic peptide belonging to the growth hormone-releasing hormone analog family. It comprises twenty-nine amino acid residues derived from the N-terminal region of natural GHRH. The molecule incorporates several non-natural substitutions that increase resistance to enzymatic degradation. These modifications extend its activity compared with the native hormone fragment. Researchers use it to study pituitary growth hormone secretion in laboratory and clinical settings. This compound is distinct from native GHRH in its stability profile.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular weight, DAC form | About 3647 Da | Varies with salt form |
| Molecular weight, non-DAC form | About 3358 Da | MOD GRF(1-29) |
| Solubility class | Water soluble | Also dissolves in polar solvents |
| Reported half-life, DAC form | About five to eight days | Values from human studies |
| Common synonyms | CJC-1295; MOD GRF(1-29) | Name depends on variant |
The distinguishing feature of the DAC form is a maleimide-containing group that reacts with the free thiol of cysteine-34 on human serum albumin. This reaction forms a covalent bond without enzymatic assistance, and it takes place after the peptide enters the bloodstream. Because albumin is abundant and long-lived, the attached peptide is carried through circulation far longer than an unmodified fragment would survive. The chemistry is a deliberate pharmacokinetic strategy rather than a change to receptor activity.
Enzymatic protection is a separate mechanism from plasma protein binding. The four substitutions in the backbone reduce recognition by dipeptidyl peptidase IV, which normally cleaves the natural hormone within minutes. Without the reactive group, this resistance still yields only a short window of activity, generally reported in the range of tens of minutes. With it, reported half-lives in early human work extended to several days. The size of that gap is the main practical distinction between the two materials.
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.
Once in circulation, the peptide binds the growth hormone-releasing hormone receptor displayed on pituitary somatotroph cells. Receptor activation couples to Gs proteins, elevates intracellular cyclic AMP, and drives protein kinase A signaling inside the cell. That cascade increases discharge of growth hormone into the bloodstream. The analog therefore operates through a receptor pathway that already exists for the body's own releasing hormone, rather than through an engineered artificial target.
Clearance profiles diverge sharply between the two versions. The albumin-binding molecule stays in plasma for several days, whereas the unmodified analog is largely gone within about half an hour in reported work. Cleavage by dipeptidyl peptidase IV is a major contributor to the short life of the unmodified sequence. These gaps mean the two versions cannot be substituted for each other in study design or in reading results side by side.
Reports on this compound commonly follow serum growth hormone and insulin-like growth factor 1 across defined time windows. Protocols differ in sampling frequency, assay platform, and participant characteristics, which makes direct comparison between publications difficult. Some work focuses on pulsatile release patterns instead of average concentrations. Whether repeated exposure alters endogenous hormone rhythms over long periods remains an open question, and the formal literature is thinner than the volume of informal commentary implies.
== External links == "Do insects have blood?". Boston Globe. October 17, 2005. Archived from the original on October 2, 2022. Bolstad, Kat (May 2, 2008). "Blue Squid Blood - Murky Water". Te Papa Tongarewa Museum of New Zealand. Archived from the original on April 2, 2015.
=== Drug interactions === Isoniazid decreases the metabolism of carbamazepine, slowing down its clearance from the body. People taking carbamazepine should have their carbamazepine levels monitored and, if necessary, have their dose adjusted accordingly. Isoniazid can also increase the amount of phenytoin in the body. The doses of phenytoin may need to be adjusted when given with isoniazid. Isoniazid may increase the plasma levels of theophylline. There are some cases of theophylline slowing down isoniazid elimination. Both theophylline and isoniazid levels should be monitored. Valproate levels may increase when taken with isoniazid. Valproate levels should be monitored and its dose adjusted if necessary. People taking isoniazid and acetaminophen are at risk of acetaminophen toxicity. Isoniazid is thought to induce a liver enzyme which causes a larger amount of acetaminophen to be metabolized to a toxic form. It is possible that isoniazid may decrease the serum levels of ketoconazole after long-term treatment. This is seen with the simultaneous use of rifampin, isoniazid, and ketoconazole.
According to Goodrich, both lineages evolved from an earlier stem group, Protosauria ("first lizards") in which he included some animals today considered reptile-like amphibians, as well as early reptiles. In 1956, D.M.S. Watson observed that the first two groups diverged very early in reptilian history, so he divided Goodrich's Protosauria between them. He also reinterpreted Sauropsida and Theropsida to exclude birds and mammals, respectively. Thus his Sauropsida included Procolophonia, Eosuchia, Millerosauria, Chelonia (turtles), Squamata (lizards and snakes), Rhynchocephalia, Crocodilia, "thecodonts" (paraphyletic basal Archosauria), non-avian dinosaurs, pterosaurs, ichthyosaurs, and sauropterygians. In the late 19th century, a number of definitions of Reptilia were offered. The biological traits listed by Lydekker in 1896, for example, include a single occipital condyle, a jaw joint formed by the quadrate and articular bones, and certain characteristics of the vertebrae. The animals singled out by these formulations, the amniotes other than the mammals and the birds, are still those considered reptiles today. The synapsid/sauropsid division supplemented another approach, one that split the reptiles into four subclasses based on the number and position of temporal fenestrae, openings in the sides of the skull behind the eyes. This classification was initiated by Henry Fairfield Osborn and elaborated and made popular by Romer's classic Vertebrate Paleontology. Those four subclasses were:
Sources: en.wikipedia.org
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==== Elicitors ==== Pst DC3000 produces a PsINF1, the INF1 in P. syringae. Hosts respond with autophagy upon detection of this elicitor. Liu et al. 2005 finds this to be the only alternative to mass hypersensitivity leading to mass programmed cell death.
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Sources: en.wikipedia.org
It is a synthetic peptide modeled on growth hormone-releasing hormone. The molecule is used in research on pituitary growth hormone secretion. It differs from the natural hormone through several stabilizing substitutions.
The DAC form carries a maleimide group that binds albumin and extends circulation time. The non-DAC form lacks this group and clears much faster. Both share the same receptor-binding core.
It targets the growth hormone-releasing hormone receptor on pituitary somatotroph cells. Activation raises cyclic AMP and promotes growth hormone release. Normal feedback pathways remain part of the response.
A maleimide moiety reacts with the thiol of cysteine-34, forming a covalent bond. The reaction occurs in circulation without enzymatic catalysis.