Everything below concerns albumin binding. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2026-01-22. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Physical form | Lyophilized white powder | Supplied as a freeze-dried solid for research use |
| Molecular weight | Approximately 3,647 Da (DAC form) | Lower for the variant lacking the albumin-binding moiety |
| Solubility | Soluble in water and aqueous buffer | Typically dissolved in sterile or bacteriostatic water |
| Typical storage temperature | −20 °C or below | Dry powder, desiccated and protected from light |
| Common analytical method | Reversed-phase HPLC with mass spectrometry | Used for purity estimation and identity confirmation |
Studies in this area generally track growth hormone pulses, insulin-like growth factor 1 concentrations, and occasionally body composition endpoints. Most published human data come from early, small trials, and questions about long-term effects remain open. Whether repeated exposure alters pituitary responsiveness over time is not settled. Analytical work relies on immunoassays for the hormones and on mass spectrometry for the peptide itself, because the two measurements answer different questions.
Binding of the peptide to the growth hormone-releasing hormone receptor on pituitary somatotrophs triggers a G protein coupled cascade that raises cyclic AMP and opens calcium channels. The result is greater secretion of growth hormone into the bloodstream. Because the peptide acts at the same receptor as the natural hypothalamic hormone, its effect is amplified pulse size rather than an entirely separate release pathway. Receptor binding alone does not determine the response, since somatostatin tone and other inputs modulate the final output.
The albumin-binding version stays in circulation for days, because covalent attachment to serum albumin shields the peptide from rapid filtration and degradation. Reported half-lives for this form fall in the range of several days. The version without the linker is cleared in minutes, with estimates often near thirty minutes in animal work. These figures come from small studies and vary with assay method, species, and route, so they are best read as approximate rather than fixed constants.
Two related forms appear under the CJC-1295 name. The simpler analogue, commonly written as modified GRF(1-29), carries the four substitutions but no additional conjugation. The second form attaches a maleimidopropionic acid linker to a lysine residue, a modification frequently called the drug affinity complex. That linker reacts with the free thiol on serum albumin to form a covalent bond. Because albumin has a long residence time in blood, the conjugated peptide stays in circulation far longer than the unconjugated analogue.
Receptor level activity follows the canonical GHRH pathway. The peptide binds the GHRH receptor, a class B G protein coupled receptor on somatotroph cells of the anterior pituitary. Binding raises intracellular cyclic AMP, which promotes calcium entry and the release of growth hormone into the bloodstream. Because the molecule acts at the same receptor as the endogenous hormone, its effect is superimposed on the natural pulsatile rhythm rather than replacing it. Whether sustained receptor occupation leads to desensitization is not fully settled.
Aspirin Ibuprofen (Advil, Nurofen) Naproxen (Aleve) There are several potential pharmacokinetic interactions between the various individual SSRIs and other medications. Most of these arise from the fact that every SSRI can inhibit certain P450 cytochrome enzymes.
Enfortumab vedotin, sold under the brand name Padcev, is an antibody-drug conjugate used for the treatment of urothelial cancer. It is a nectin-4-directed antibody and microtubule inhibitor conjugate. Enfortumab refers to the monoclonal antibody part, and vedotin refers to the payload drug (MMAE) and the linker. The most common side effects include fatigue, peripheral neuropathy (nerve damage resulting in tingling or numbness), decreased appetite, rash, alopecia (hair loss), nausea, altered taste, diarrhea, dry eye, pruritus (itching) and dry skin. The fully humanized antibody was created by scientists at Agensys (part of Astellas) using Xenomice from Amgen; the linker technology holding the antibody and the toxin together was provided by and licensed from Seattle Genetics. The U.S. Food and Drug Administration (FDA) considers it to be a first-in-class medication.
In addition, a violent anti-Peruvian campaign developed in the Ecuadorian press, newspapers and radio broadcasters became very contemptuous and very hostile street demonstrations against Peruvians were encouraged, attacking the Peruvian Consulate in Guayaquil. The way of carrying out this action by Ecuador, in numerical inferiority and with a fleet of weapons, quickly resolved the conflict in favor of Peru with serious consequences in terms of building national identity.
Aroa Biosurgery Limited (formerly Mesynthes Limited) is a regenerative medicine company that develops, manufactures and distributes products for wound healing and soft tissue reconstruction. Aroa Biosurgery is headquartered in Auckland, New Zealand with a US office in San Diego, CA, and is listed on the Australian Securities Exchange (ASX: ARX). The company, originally known as Mesynthes Limited, was founded in 2008 by Veterinarian Surgeon Dr Brian Ward (BVSc). The company develops and commercializes products based on its proprietary ovine forestomach matrix technology platform with products in wound healing (Endoform, Natural, Endoform, Antimicrobial and Symphony) as well as plastics and reconstructive surgery (Myriad Matrix, Myriad Forme, Myriad Morcells, Ovitex PRS) and repair of hernia (Ovitex and Myriad Ultra).
Sources: en.wikipedia.org
The better way of removing ammonium sulfate from the protein is mixing the precipitate protein in a buffer containing a mixture of SDS, Tris-HCl, and phenol and centrifuging the mixture. The precipitate that comes out of this centrifugation will contain salt-less concentrated protein.
Gold nanoparticles show potential as intracellular delivery vehicles for antisense oligonucleotides (single and double stranded DNA) by providing protection against intracellular nucleases and ease of functionalization for selective targeting.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
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.
It has not been approved by major regulatory agencies for any therapeutic indication. Material sold under this name is typically distributed for laboratory research only. Clinical use is not supported by large controlled trials.
Early human studies of the albumin-binding form reported circulation half-lives on the order of several days. The value depends on assay method and study design. Estimates for the form without the binding moiety are considerably shorter.
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.