This is a working overview of GRF(1-29), written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2025-10-09. Anything still debated is marked as such rather than presented as settled.
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.
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 dividing feature between the two forms is a maleimide-based drug affinity complex, abbreviated DAC. In the DAC-bearing version, a linker attaches the peptide to serum albumin after administration, and that association slows removal from plasma. The version lacking DAC appears in catalogs as MOD GRF(1-29) or tetrasubstituted GRF(1-29). Because informal writing treats both as one item, comparisons drawn from such sources routinely blend measurements taken from two molecules with substantially different behavior.
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.
| 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 |
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.
CJC-1295 is a synthetic peptide built as a long-acting analogue of growth hormone-releasing hormone. Its backbone matches the first twenty-nine residues of the natural human hormone, with four amino acid substitutions added to slow enzymatic breakdown. A reactive maleimide group, commonly termed the drug affinity complex, allows the peptide to attach to circulating albumin after administration. That albumin attachment keeps the molecule in the bloodstream for an extended period instead of being cleared within minutes.
The compound emerged from work at a Canadian biotechnology firm in the early 2000s. Early human studies examined its effect on growth hormone and insulin-like growth factor 1 in healthy volunteers and in people with HIV-associated fat redistribution. Reports described sustained increases in both markers after a single injection. Development did not advance to regulatory approval, and the clinical programme was later discontinued. The molecule is now encountered mainly as a research chemical rather than a marketed medicine.
Knowledge Training and experience Reagents and materials preparation Characteristics of operational steps Calibration, quality control, and proficiency testing materials Test system troubleshooting and equipment maintenance Interpretation and judgment The Centers for Medicare & Medicaid Services (CMS) has the primary responsibility for the operation of the CLIA Program. Within CMS, the program is implemented by the Center for Medicaid and State Operations, Survey and Certification Group, and the Division of Laboratory Services. List of CLIA test complexity categorizations:
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== History == Doxepin was discovered in Germany in 1963 and was introduced in the United States as an antidepressant in 1969. It was subsequently approved at very low doses in the United States for the treatment of insomnia in 2010.
Sources: en.wikipedia.org
=== Category:EC 6.2 (form carbon–sulfur bonds) === EC 6.2.1.1: Acetate—CoA ligase EC 6.2.1.2: Medium-chain acyl—CoA ligase EC 6.2.1.3: Long-chain-fatty-acid—CoA ligase EC 6.2.1.4: Succinate—CoA ligase (GDP-forming) EC 6.2.1.5: Succinate—CoA ligase (ADP-forming) EC 6.2.1.6: Glutarate—CoA ligase EC 6.2.1.7: Cholate—CoA ligase EC 6.2.1.8: Oxalate—CoA ligase EC 6.2.1.9: Malate—CoA ligase EC 6.2.1.10: Acid—CoA ligase (GDP-forming) EC 6.2.1.11: Biotin—CoA ligase EC 6.2.1.12: 4-Coumarate—CoA ligase EC 6.2.1.13: Acetate—CoA ligase (ADP-forming) EC 6.2.1.14: 6-carboxyhexanoate—CoA ligase EC 6.2.1.15: Arachidonate—CoA ligase EC 6.2.1.16: Acetoacetate—CoA ligase EC 6.2.1.17: Propionate—CoA ligase EC 6.2.1.18: Citrate—CoA ligase EC 6.2.1.19: Long-chain-fatty-acid-luciferin-component ligase EC 6.2.1.20: Long-chain-fatty-acid-(acyl-carrier-protein) ligase EC 6.2.1.21: Transferred entry: 6.2.1.30 EC 6.2.1.22: (citrate (pro-3S)-lyase) ligase EC 6.2.1.23: Dicarboxylate—CoA ligase EC 6.2.1.24: Phytanate—CoA ligase EC 6.2.1.25: Benzoate—CoA ligase EC 6.2.1.26: o-Succinylbenzoate—CoA ligase EC 6.2.1.27: 4-hydroxybenzoate—CoA ligase EC 6.2.1.28: 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate—CoA ligase EC 6.2.1.29: Transferred entry: 6.2.1.7 EC 6.2.1.30: Phenylacetate—CoA ligase EC 6.2.1.31: 2-furoate—CoA ligase EC 6.2.1.32: Anthranilate—CoA ligase EC 6.2.1.33: 4-chlorobenzoate—CoA ligase EC 6.2.1.34: trans-Feruloyl—CoA synthase EC 6.2.1.35: ACP-SH:acetate ligase EC 6.2.1.36: 3-hydroxypropionyl-CoA synthase EC 6.2.1.37: 3-hydroxybenzoate—CoA ligase EC 6.2.1.38: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase EC 6.2.1.39: (butirosin acyl-carrier protein)—L-glutamate ligase EC 6.2.1.40: 4-Hydroxybutyrate—CoA ligase EC 6.2.1.41: 3-((3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl)propanoate—CoA ligase EC 6.2.1.42: 3-oxocholest-4-en-26-oate—CoA ligase EC 6.2.1.43: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase EC 6.2.1.44: 3-(methylthio)propionyl—CoA ligase EC 6.2.1.45: E1 ubiquitin-activating enzyme EC 6.2.1.46: L-allo-Isoleucine—holo-CmaA peptidyl-carrier protein ligase EC 6.2.1.47: Medium-chain-fatty-acid-(acyl-carrier-protein) ligase EC 6.2.1.48: Carnitine—CoA ligase EC 6.2.1.49: Long-chain fatty acid adenylyltransferase FadD28 EC 6.2.1.50: 4-hydroxybenzoate adenylyltransferase FadD22 EC 6.2.1.51: 4-hydroxyphenylalkanoate adenylyltransferase FadD29 EC 6.2.1.52: L-Firefly luciferin—CoA ligase EC 6.2.1.53: L-Proline—L-prolyl-carrier protein ligase EC 6.2.1.54: D-Alanine—D-alanyl-carrier protein ligase EC 6.2.1.55: E1 SAMP-activating enzyme
==== Context ==== The announcement of the new cabinet is an attempt to resolve a political crisis between Pedro Castillo and the Congress of the Republic. On 24 November 2022, President Castillo delivered a speech to the nation in which he announced that he accepted the resignation of Aníbal Torres and also the appointment of a new cabinet. The resigning Prime Minister wanted to provoke a vote of confidence in Congress so that it would analyze a constitutional reform project to annul Congress in order to trigger referendums, particularly on the Constituent Assembly, a historic project of Castillo's, but the vote of confidence was denied by the presidency of Congress, dominated by the centre-right and the right. In that same speech, Pedro Castillo evokes the interpretation of Congress's decision not to allow the vote of confidence desired by the President of the council as an "express refusal of confidence" and considers this cabinet change legitimate.
Lysine malonylation (Kmal, maK), protein malonylation or malonylation, is a reversible post-translational modification (PTM) in eukaryotic and prokaryotic cells, in which a malonyl group (–CO–CH2–COOH) is added to a lysine (K) residue of a protein. It was first identified in 2011 by Peng et al. as an evolutionarily conserved modification and belongs to the acidic acyl modifications such as succinylation and glutarylation. As a dynamically regulated modification, it responds to conditions such as stress responses, metabolic processes, and mutations, thereby influencing the charge, structure, and function of proteins. This involves, among other things, the metabolic pathways of glucose and fatty acids as well as histone-mediated gene regulation, and is increasingly associated with immune regulation, angiogenesis, osteoarthritis, cancer and metabolic diseases such as obesity and type 2 diabetes. Its biological significance is increasingly recognized, but many aspects of its regulation and function remain unresolved, so that its therapeutic potential is still unexplored.
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.
No. It is a laboratory-synthesized analog built on a fragment of the natural hormone. The natural peptide is shorter-lived and lacks the stabilizing substitutions found in the synthetic version.