The short version of GHRH analog fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-01-08. Anything still debated is marked as such rather than presented as settled.
CJC-1295 is the name used for a synthetic peptide modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. The compound was described by a Canadian drug discovery company in the mid-2000s as a long-acting research tool. Two closely related molecules share the name in practice: one carries a drug affinity complex, or DAC, group, and one does not. The distinction matters because the two behave differently in circulation.
The peptide backbone corresponds to GRF(1-29), the first 29 residues of native growth hormone-releasing hormone, which retains most of the receptor-activating activity of the full-length molecule. Four substitutions distinguish the analog from the natural sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27. These changes slow cleavage by dipeptidyl peptidase IV, the enzyme that degrades native hormone in plasma within minutes. The outcome is improved enzymatic stability combined with a still brief residence time when no additional modification is present.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic peptide | GHRH analog, not a steroid |
| Backbone length | 29 amino acids | Based on GRF(1-29) |
| Substitutions | Four positions | D-Ala2, Gln8, Ala15, Leu27 |
| Appearance | White to off-white powder | Typical lyophilized research material |
| Common synonyms | Modified GRF(1-29) | Usage varies between sources |
Lyophilized peptide powder is comparatively stable when kept dry, cold, and protected from light. Once dissolved, the molecule is vulnerable to deamidation, oxidation, and aggregation, with the rate depending on pH, buffer composition, and temperature. Alkaline conditions and repeated freeze-thaw cycles accelerate loss of the intact peptide. The methionine present in the native sequence is a known oxidation site, which is one reason it was replaced in the modified fragment. Suppliers typically recommend cold storage of solutions and use within a short window.
Analytical confirmation usually relies on reversed-phase high-performance liquid chromatography for purity and on liquid chromatography coupled to mass spectrometry for identity. Mass data reveal the expected molecular mass and can flag truncated or oxidized species. Amino acid analysis and peptide mapping provide sequence-level verification. Immunoassays are used in some biological matrices, but antibodies raised against one releasing-hormone analog may cross-react with another. Reported purity figures depend heavily on the method used, so comparisons between suppliers require matching the analytical approach.
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 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.
Four amino acid substitutions separate the modified backbone from the parent GRF(1-29) sequence. These changes reduce recognition by dipeptidyl peptidase IV and related proteases, extending the interval before degradation. Development work in this area sought longer-acting GHRH analogs for endocrine investigation. Published descriptions treat the substitution set as a defining property of the core sequence, while the albumin-binding linker is described separately as an optional addition to that same backbone.
CJC-1295 is a synthetic peptide analog of growth hormone-releasing hormone, constructed on the 29-amino-acid fragment designated GRF(1-29). The name began as an internal development code during the 1990s and later spread through research supply catalogs and discussion forums. The molecule does not occur in nature; its sequence is engineered rather than isolated from tissue. Two related compounds are sold under this single label, and they differ by one appended chemical group that strongly influences how long the peptide remains in circulation.
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.
Downstream of growth hormone, the liver and other tissues increase production of insulin-like growth factor 1, a mediator of many growth-promoting effects. Studies have documented elevated levels of both hormones after dosing, and the rise from the long-acting form persists longer than that produced by shorter-acting analogues. What remains unclear is whether sustained elevation of these markers translates into meaningful clinical benefit, and whether prolonged exposure carries risks that short trials could not detect.
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.
In the 1580s, under the direction of Thomas Digges and championed by Sir Walter Raleigh, early port infrastructure work commenced to address siltation through the use of sluices and the development of an enclosed pool of water known as the Great Pent, by means of which the harbour could be periodically scoured. The Great Pent was formed by the construction of a cross wall across the existing natural shingle lagoon at the mouth of the River Dour: the work was largely undertaken by labourers from Romney Marsh, using skills honed in the construction of seawalls. The project has been described as "one of the most successful engineering enterprises of [Queen] Elizabeth's reign". The later construction of Wellington Dock, designed by James Walker in the early 1830s, occupies the approximate footprint of the Great Pent. After the threats of the Napoleonic Wars at the beginning of the 19th century, the Admiralty selected Dover as the most suitable location of a harbour of refuge for the fleet between the dockyards of Chatham and Portsmouth. In 1847 construction began on the Admiralty Pier. Envisaged as the Western Arm of the proposed haven, completion of the massive first stage in 1871 effectively stopped the silting of the harbour mouth as it cut off the drift of shingle from the direction of Folkestone. The Admiralty Pier was constructed using a foundation of Portland stone blocks surmounted by granite and durable Bramley Fall stone on the seaward facing exterior. Stothert & Pitt's 1885 Price Book records Messers H.
== External links == Bak Sangmee, From Strange Bitter Concoction to Romantic Necessity: The Social History of Coffee Drinking in South Korea. (Korea Journal Vol.45. No.2 Summer, 2005 pp. 37~59) Korea Coffee Market, Terarosa Coffee, Yunson, Lee Korea's coffee culture, korea.net Episode #33: The History of Coffee in Korea, KBS World The History of Coffee in Korea, Daniel Gray Korean Coffee Culture 101 – History & Timeline Archived 2016-12-06 at the Wayback Machine Café Culture in Seoul, Korea JungHee Jang, Korean Café Culture: What Korean Cafés Mean to Koreans Cultural Meaning and Power of Starbucks in South Korea
that the physical action of crosslinking brings the ectodomain into such a conformation that is required for intracellular tyrosine phosphorylation events to ensue (i.e. these events serve as the requirements for receptor activation and eventual maintenance of blood glucose homeostasis). Visualization of full length IR complexes is not yet available due to many constraints. Visualization of full length IR–insulin complexes is not yet available due to flexible link of transmembrane (TM) domains with extracellular domain and intracellular domain. The transmembrane (TM) domains are critical for activation and downstream signaling. Stabilization of TM domains may be result of phosphatidylinositol. Meanwhile, visualization of full length IR–downstream proteins is challenging because of transient nature of association, the phosphorylation receptor requirement, and the unfixed relative orientation. Applying cryo-EM and molecular dynamics simulations of receptor reconstituted in nanodiscs, the structure of the entire dimeric insulin receptor ectodomain with four insulin molecules bound was visualized, therefore confirming and directly showing biochemically predicted 4 binding locations.
Sources: en.wikipedia.org
== Chemistry == The drug is composed of three monoclonal antibodies (mAbs), initially harvested from mice exposed to Ebola virus proteins, that have been chimerized with human constant regions. The components are chimeric monoclonal antibody c13C6 from a previously existing antibody cocktail called "MB-003" and two chimeric mAbs from a different antibody cocktail called ZMab, c2G4, and c4G7. ZMapp is manufactured in the tobacco plant Nicotiana benthamiana in the bioproduction process known as "pharming" by Kentucky BioProcessing, a subsidiary of Reynolds American.
=== Solvent interface trapping method (SITM) === As reported by a group led by D. H. Adamson, graphene can be produced from natural graphite while preserving the integrity of the sheets using the solvent interface trapping method (SITM). SITM uses a high-energy interface, such as oil and water, to exfoliate graphite to graphene. Stacked graphite delaminates, or spreads, at the oil/water interface to produce few-layer graphene in a thermodynamically favorable process in much the same way as small molecule surfactants spread to minimize the interfacial energy. In this way, graphene behaves like a 2D surfactant. SITM has been reported for a variety of applications such conductive polymer-graphene foams, conductive polymer-graphene microspheres, conductive thin films and conductive inks.
==== Indirect immunofluorescence (IDIF) ==== Patients with high concentration of antibodies show intercellular, intraepidermal antibodies as well as along the dermoepidermal junction. Patients with low concentration of antibodies only present with them inside the cells (intercellular). If the results are negative, perform the additional assays regardless. Cases have been confirmed that reported with initial negative DIF and IDIF tests.
Willard Marriott gained franchise rights for Washington, D.C., Baltimore and Richmond. Subsequently, he moved to Washington to open a root beer stand with Hugh Colton. These stands subsequently became Hot Shoppes, paving the way for the later creation of one of the largest hospitality corporations in the world. As of 1933, A&W had a total of 171 stands, increasing to 260 by 1941. A&W survived the Great Depression and labor shortages during World War II but benefitted from the post-war recovery of the American economy, with fast food and drive-in restaurants beginning to take shape. The first franchise convention was held in La Crosse, Wisconsin in 1949, but was limited to Wisconsin franchisees.
Sources: en.wikipedia.org
No. It is a laboratory-made analog of growth hormone-releasing hormone. The natural hormone is a 44-residue peptide, while the analog is built on a shorter 29-residue fragment.
The original material included a linker that binds serum albumin. A later variant removed that linker to reduce the duration of action. Catalogs and papers did not consistently adopt separate names, so both remain widely labeled with the same term.
The amino acid sequence and the presence or absence of the linker group. Mass measured by spectrometry gives an independent check that separates the two forms.
The two share the same 29-amino-acid backbone. CJC-1295 carries an additional albumin-binding moiety that markedly extends its residence time in circulation, while the form without that moiety clears faster. Literature sometimes applies the name loosely to either variant.