The short version of GRF(1-29) fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-06-12. 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.
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.
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.
Characterization of this peptide relies on a small set of routine techniques. Reversed-phase high-performance liquid chromatography separates the target from truncated or oxidized by-products and yields a purity estimate when paired with ultraviolet detection near 214 nanometers. Mass spectrometry, either electrospray coupled to liquid chromatography or matrix-assisted laser desorption, confirms that the observed mass matches the value calculated for the expected sequence. Amino acid analysis, and enzymatic digestion followed by fragment mapping, are used when the sequence itself rather than the mass requires verification.
Stability depends heavily on physical state. A lyophilized powder kept dry, desiccated, and shielded from light typically holds its integrity for months to years at minus twenty degrees Celsius, and longer at minus eighty. Once dissolved, the peptide becomes far more vulnerable, since peptide bond hydrolysis, oxidation of susceptible residues, and aggregation all proceed faster in solution. Buffers near neutral pH are generally gentler than strongly acidic or alkaline conditions. Repeated freeze-thaw cycles and exposure to air-liquid interfaces during vigorous mixing cause losses that are easy to overlook.
Verification matters because research peptides vary widely in quality. A certificate of analysis is only as reliable as the method behind it, and a single chromatographic trace reveals little about counter-ions, residual solvents, or water content. Independent laboratories commonly pair mass confirmation with chromatographic purity and, where relevant, quantify water along with acetate or trifluoroacetate content. Reported purity figures are not standardized across suppliers, so a stated value such as ninety-eight percent is not directly comparable unless the analytical method, column, and detection wavelength accompany it.
The delayed time to peak levels (2–3 hours) and long elimination half-life (12 hours) of suvorexant are less than ideal for an insomnia medication as they result in a delayed onset of effect and significant next-day side effects such as daytime sedation. Orexin receptor antagonists with shorter half-lives and faster onsets of action are theoretically more optimal for therapeutic use as sleep aids. The ideal insomnia medication would not have a duration of action extending beyond about 8 hours. Relative to suvorexant, daridorexant has a shorter half-life (8 hours) while lemborexant has a longer half-life (17–55 hours). However, although lemborexant has a longer terminal elimination half-life than suvorexant, it appears to be more rapidly cleared in the earlier phases of elimination. The investigational agents seltorexant and vornorexant, which are still in clinical trials, have comparatively very short half-lives in the range of 1.5 to 3 hours.
VP-13 operating PB2Y-3s from 26 February to 22 June 1944 VP-16 operating PBM-3Ds from 7 June to 1 August 1944 VP-21 operating PBM-3Ds from 19 August to 17 October 1944 and from 15 July to 11 September 1945 VP-23 operating PBY-5As from 20 August 1944 to 9 April 1945 VP-MS-6 operating PBM-5Es from 1 February 1948 in support of Operation Sandstone VP-102 operating PB2Y-3s from 3 February to 30 August 1944 VP-202 operating PBM-3Ds from 24 February to 1 March 1944 VPB-19 operating PBM-3Ds from 2 November 1944 to 12 February 1945 and 6 March 1945 to January 1946 VPB-22 operating PBM-3Ds from 10 October to 30 November 1944 and from 25 June to 7 August 1945
== External links == "Rusfertide ( Code - C162883 )". EVS Explore. "Rusfertide Acetate ( Code - C180660 )". EVS Explore. Clinical trial number NCT05210790 for "A Phase 3 Study of Rusfertide in Patients With Polycythemia Vera (VERIFY)" at ClinicalTrials.gov
Sources: en.wikipedia.org
Infections with carbapenem-resistant Klebsiella pneumoniae were associated with organ/stem cell transplantation, mechanical ventilation, exposure to antimicrobials, and overall longer length of stay in hospitals. People most likely to acquire carbapenem-resistant bacteria are those already receiving medical attention. In a study carried out at Sheba medical center, there was a trend toward worse Charleson Comorbidity scores in patients who acquired CRKP during ICU stay. Those at highest risk are patients receiving an organ or stem cell implantation, use of mechanical ventilation, or have to have an extended stay in the hospital along with exposure to antimicrobials. A study performed in Singapore, on the acquisition of ertapenem-resistant Enterobacteriaceae to the acquisition of CRE. revealed that exposure to antibiotics, especially fluoroquinolones and previous hospitalization dramatically increased the risk of acquisition carbapenem-resistant bacteria. This study found that carbapenem-resistant acquisition has a significantly higher mortality rate and poorer clinical response compared to that of the ertapenem-resistance acquisition. Bacteruria (also known as urinary tract infection) caused by CRKp and CSKp have similar risk factors. These include prior antibiotic use, admittance to an ICU, use of a permanent urinary catheter, and previous invasive procedures or operations.
Nα-acetylpeptide + CoA Thus, the two substrates of this enzyme are acetyl-CoA and peptide, whereas its two products are Nα-acetylpeptide and CoA. Since 2016, the different enzymes that used to be in this class are separated into NatA-NatF (EC 2.3.1.254 to EC 2.3.1.259). These enzymes belong to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:peptide Nα-acetyltransferase. Other names in common use include beta-endorphin acetyltransferase, peptide acetyltransferase, protein N-terminal acetyltransferase, NAT, Nalpha-acetyltransferase, amino-terminal amino acid-acetylating enzyme, and acetyl-CoA:peptide alpha-N-acetyltransferase.
X-rays can be passed through the body and used in medical radiography and fluoroscopy to differentiate interior structures that have varying degrees of opaqueness. Magnetic resonance imaging, computed tomography, and ultrasound imaging have all enabled the examination of internal structures in unprecedented detail to a degree far beyond the imagination of earlier generations. Infrared and ultraviolet analysis, computer image processing, fractal analysis, metrological analysis using image analysis methods are modern methods useful especially in neuroanatomical research.
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.