If you have been reading about CJC-1295 and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Last reviewed on 2025-08-19. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
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.
| 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.
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.
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.
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.
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.
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.
== Gene structure and regulation == CCN1 is located at human chromosome 1p22.3, whereas the mouse CCN1 gene is located at chromosome 3, 72.9cM. The mouse CCN1 coding region spans ~3.2 Kb, containing 5 exons interspaced with 4 introns. The first exon encodes 5’-UTR sequence and the first several amino acids in the secretory signal peptide. The remaining four exons each encode a distinct CCN1 domain. The 5th exon also contains the 3’-UTR sequences, which has 5 copies of AU-rich elements that confers a short mRNA half life, and a mir-155 target site. The CCN1 promoter is a TATA box containing promoter, with binding sites for many transcription factors including AP1, ATF, E2F, HNF3b, NF1, NFκB, SP1, and SRF, and 2 poly(CA) stretches that may form Z-DNA structure. Transcriptional activation of CCN1 is exquisitely sensitive to a wide range of environmental perturbations, including stimulation by platelet-derived growth factor and basic fibroblast growth factor, transforming growth factor β1 (TGF-β1), growth hormone, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA), cAMP, vitamin D3, estrogen and tamoxifen, angiotensin II, hypoxia, UV light, and mechanical stretch.
3-Methoxyphencyclidine (3-MeO-PCP) is a dissociative anesthetic of the arylcyclohexylamine class structurally related to PCP. It has been sold online as a designer drug. It has been used across Europe and the United States. It acts mainly as an NMDA receptor antagonist, though it has also been found to interact with the sigma σ1 receptor and the serotonin transporter.
=== Quantitative sudomotor axon reflex test === The quantitative sudomotor axon reflex test (QSART) was developed in 1983 by Phillip Low as a quantitative method for the identification of localized postganglionic sudomotor dysfunction. Three-compartment sweat capsules are placed on the forearm, proximal and distal leg, as well as the dorsum of the foot. The outer compartment of the capsule is filled with a 10% acetylcholine solution, while nitrogen gas is released steadily onto the skin within the inner compartment. The middle compartment acts as a buffer between the inner and outer compartments to prevent direct stimulation of sweat glands or leakage of the acetylcholine solution. The outflow humidity of the nitrogen gas after passing across the skin is measured by a hygrometer. Once a stable baseline of outflow humidity is reached, iontophoresis of the acetylcholine fluid is initiated by using a 2mA electric current to deliver the acetylcholine into the dermal skin layers. The acetylcholine binds to sweat glands (direct sweat response), and nicotinic and muscarinic receptors on the sudomotor nerve terminals, which transmit the action potential antidromically to axon branch points and then orthodromically to adjacent sudomotor nerves and glands (indirect sweat response). Sweat production is measured as the change in relative humidity over time. The temporal resolution, magnitude, and onset latency of the sweat response are digitally recorded and analyzed using specialized software. QSART is sensitive and specific for detecting postganglionic small fiber dysfunction.
Sources: en.wikipedia.org
. As of 1994, limited information existed on the acute toxicity of carbonyl sulfide in humans and in animals. High concentrations (above 1000 ppm) can cause sudden collapse, convulsions, and death from respiratory paralysis. Occasional fatalities have been reported, practically without local irritation or olfactory warning. In tests with rats, 50% animals died when exposed to 1400 ppm of COS for 90 minutes, or at 3000 ppm for 9 minutes. Limited studies with laboratory animals also suggest that continued inhalation of low concentrations (around 50 ppm for up to 12 weeks) does not affect the lungs or the heart. Carbonyl sulfide is a potential alternative fumigant to methyl bromide and phosphine. In some cases, however, residues on the grain result in flavours that are unacceptable to consumers, such as in barley used for brewing.
After the reforms ended in 1909, the Indian Army was organised along British lines, although it was always behind in terms of equipment. An Indian Army division consisted of three brigades each of four battalions. Three of these battalions were of the Indian Army, and one British. The Indian battalions were often segregated, with companies of different tribes, castes or religions. One and a half million volunteers came forward from the estimated population of 315 million in the Indian subcontinent. Regimental battalions were not permanently allocated to particular divisions or brigades, but instead spent some years in one formation, and were then posted to another elsewhere. This rotating arrangement was intended both to provide all units with experience of active service on the Frontier, and to prevent them becoming 'localised' in static regimental stations. In contrast, the divisional locations remained constant.
Before entering metamorphosis, the larvae expel a transparent glue from their salivary gland through their mouth, which solidifies within a few seconds and fixes them into a substrate. Then the larvae encapsulate in the puparium and undergo a four-day-long metamorphosis (at 25 °C), after which the adults eclose (emerge).
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.