The short version of CJC-1295 fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2026-04-18 and is reviewed periodically as new material appears.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Peptide class | Synthetic GHRH analogue | Built on a 29 residue sequence |
| Primary target | GHRH receptor (GHRHR) | Class B G protein coupled receptor |
| Unconjugated half life | Minutes | Limited by protease degradation |
| Key modification | Four residue substitutions | Positions 2, 8, 15 and 27 |
| Common synonym | Modified GRF(1-29) | Usually denotes the form without DAC |
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 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.
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.
The nasal cavity is highly vascularized, allowing efficient transfer of molecules directly to the nervous system. Compared to other administration routes, nasal drug delivery increases bioavailability and reduces systemic exposure risks. The nasal cavity's slightly acidic environment and enzymes can affect drug degradation, making delivery systems with neutral to acidic pH ideal. The respiratory region, with its large surface area and high vascularization, is the primary site for drug absorption into systemic circulation. Targeting the olfactory region enhances nose-to-brain drug delivery, as particles can travel via the olfactory nerve to the brain. This route offers potential for treating brain diseases and mental health conditions.
Rapid Communications in Mass Spectrometry (RCM) is a biweekly peer-reviewed scientific journal published since 1987 by John Wiley & Sons. It covers research on all aspects of mass spectrometry. According to the Journal Citation Reports, the journal has a 2020 impact factor of 2.419.
=== 1992–1993: Dirt === In March 1992, the band returned to the studio. With new songs written primarily on the road, the material has an overall darker feel than Facelift, with six of the album's thirteen songs dealing with the subject of addiction. "We did a lot of soul searching on this album. There's a lot of intense feelings." Cantrell said, "We deal with our daily demons through music. All of the poison that builds up during the day we cleanse when we play." On September 29, 1992, Alice in Chains released its second album, Dirt. The album peaked at number six on the Billboard 200 and since its release has been certified 5× platinum by the RIAA, making Dirt the band's highest selling album to date. The album was a critical success, with Huey praising the album as a "major artistic statement, and the closest they ever came to recording a flat-out masterpiece." Chris Gill of Guitar World called Dirt "huge and foreboding, yet eerie and intimate", and "sublimely dark and brutally honest."
Sources: en.wikipedia.org
Nicotinic acid adenine dinucleotide phosphate (NAADP) is a Ca2+-mobilizing second messenger synthesised in response to extracellular stimuli. Like its mechanistic cousins, IP3 and cyclic adenosine diphosphoribose (Cyclic ADP-ribose), NAADP binds to and opens Ca2+ channels on intracellular organelles, thereby increasing the intracellular Ca2+ concentration which, in turn, modulates sundry cellular processes (see Calcium signalling). Structurally, it is a dinucleotide that only differs from the house-keeping enzyme cofactor, NADP by a hydroxyl group (replacing the nicotinamide amino group) and yet this minor modification converts it into the most potent Ca2+-mobilizing second messenger yet described. NAADP acts across phyla from plants to humans.
=== Motility assays === Agarose is sometimes used instead of agar to measure microorganism motility and mobility. Motile species will be able to migrate, albeit slowly, throughout the porous gel and infiltration rates can then be visualized. The gel's porosity is directly related to the concentration of agar or agarose in the medium, so different concentration gels may be used to assess a cell's swimming, swarming, gliding and twitching motility. Under-agarose cell migration assay may be used to measure chemotaxis and chemokinesis. A layer of agarose gel is placed between a cell population and a chemoattractant. As a concentration gradient develops from the diffusion of the chemoattractant into the gel, various cell populations requiring different stimulation levels to migrate can then be visualized over time using microphotography as they tunnel upward through the gel against gravity along the gradient.
The convergent orientation of the catalytic triad in the active site of serine and cysteine proteases independently in over 20 enzyme superfamilies. The use of an N-terminal threonine for proteolysis. The existence of distinct families of carbonic anhydrase is believed to illustrate convergent evolution. The use of (Z)-7-dodecen-1-yl acetate as a sex pheromone by the Asian elephant (Elephas maximus) and by more than 100 species of Lepidoptera. The biosynthesis of plant hormones such as gibberellin and abscisic acid by different biochemical pathways in plants and fungi. The protein prestin that drives the cochlea amplifier and confers high auditory sensitivity in mammals, shows numerous convergent amino acid replacements in bats and dolphins, both of which have independently evolved high frequency hearing for echolocation. This same signature of convergence has also been found in other genes expressed in the mammalian cochlea The repeated independent evolution of nylonase in two different strains of Flavobacterium and one strain of Pseudomonas. The myoglobin from the abalone Sulculus diversicolor has a different structure from normal myoglobin but serves a similar function — binding oxygen reversibly. "The molecular weight of Sulculus myoglobin is 41kD, 2.5 times larger than other myoglobins." Moreover, its amino acid sequence has no homology with other invertebrate myoglobins or with hemoglobins, but is 35% homologous with human indoleamine dioxygenase (IDO), a vertebrate tryptophan-degrading enzyme. It does not share similar function with IDO.
Sources: en.wikipedia.org
The names are often used interchangeably in casual writing, but they are not strictly identical. Modified GRF(1-29) refers to the unconjugated analogue carrying only the four substitutions. The version sold as CJC-1295 with DAC includes the albumin binding linker and clears much more slowly.
DAC stands for drug affinity complex, a term describing the maleimidopropionic acid linker. This group forms a covalent bond with the cysteine residue on serum albumin after administration. The resulting adduct is what extends the circulating half life from minutes to days.
No. It is entirely synthetic and does not correspond to any known endogenous peptide. The design starts from human growth hormone releasing hormone and introduces deliberate substitutions. Any biological effect comes from mimicking the natural hormone at its receptor.
Reported values cluster in the range of several days, reflecting slow release from the albumin complex. Estimates differ across species and assay platforms. The figure describes circulation time in study settings rather than a fixed property.