The short version of GHRH analog fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2025-08-06. Anything still debated is marked as such rather than presented as settled.
The peptide backbone corresponds to GRF(1-29), the first 29 residues of native growth hormone-releasing hormone, which retains most of the receptor-activating activity of the full-length molecule. Four substitutions distinguish the analog from the natural sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27. These changes slow cleavage by dipeptidyl peptidase IV, the enzyme that degrades native hormone in plasma within minutes. The outcome is improved enzymatic stability combined with a still brief residence time when no additional modification is present.
Naming in this area is inconsistent, and readers should treat product labels with care. In much of the literature and in vendor catalogs, the unqualified term refers to the albumin-binding version, while the version lacking the DAC group appears as modified GRF(1-29), mod GRF(1-29), or the same name with a without-DAC qualifier. Because one abbreviation has been applied to both materials, the only reliable way to identify a sample is to check the stated sequence and the presence of the linker.
CJC-1295 is the name used for a synthetic peptide modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. The compound was described by a Canadian drug discovery company in the mid-2000s as a long-acting research tool. Two closely related molecules share the name in practice: one carries a drug affinity complex, or DAC, group, and one does not. The distinction matters because the two behave differently in circulation.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic peptide | GHRH analog, not a steroid |
| Backbone length | 29 amino acids | Based on GRF(1-29) |
| Substitutions | Four positions | D-Ala2, Gln8, Ala15, Leu27 |
| Appearance | White to off-white powder | Typical lyophilized research material |
| Common synonyms | Modified GRF(1-29) | Usage varies between sources |
Analytical confirmation usually relies on reversed-phase high-performance liquid chromatography for purity and on liquid chromatography coupled to mass spectrometry for identity. Mass data reveal the expected molecular mass and can flag truncated or oxidized species. Amino acid analysis and peptide mapping provide sequence-level verification. Immunoassays are used in some biological matrices, but antibodies raised against one releasing-hormone analog may cross-react with another. Reported purity figures depend heavily on the method used, so comparisons between suppliers require matching the analytical approach.
The two variants differ dramatically in how long they persist in circulation. The form lacking the albumin-binding group has a plasma half-life measured in tens of minutes, comparable to the natural hormone fragment. The version carrying the drug affinity complex binds albumin and shows a half-life of roughly six to eight days in human studies. That figure comes from small trials that tracked hormone levels over extended periods. The physiological consequences of sustained versus pulsatile stimulation are still debated and the literature does not settle the point.
Two principal forms appear in the literature and in research supply. One carries a drug affinity complex, a maleimide-based group that forms a covalent bond with circulating albumin. This linkage slows clearance and produces a long-lasting elevation of peptide levels. The other form lacks that group and is often labeled MOD GRF(1-29). It has a much shorter circulation time. Both variants retain the same core receptor-binding sequence. Reported half-lives differ substantially between the two.
At the pituitary, the peptide binds the growth hormone-releasing hormone receptor on somatotroph cells. Receptor activation raises intracellular cyclic AMP and triggers release of stored growth hormone. Somatostatin and other hypothalamic signals modulate this response. Negative feedback from insulin-like growth factor 1 also influences output. The same regulatory architecture operates with the native hormone. Whether the synthetic analog alters feedback dynamics over repeated exposure remains an open question. Most published receptor work uses cell models rather than intact human systems.
CJC-1295 is a synthetic peptide belonging to the growth hormone-releasing hormone analog family. It comprises twenty-nine amino acid residues derived from the N-terminal region of natural GHRH. The molecule incorporates several non-natural substitutions that increase resistance to enzymatic degradation. These modifications extend its activity compared with the native hormone fragment. Researchers use it to study pituitary growth hormone secretion in laboratory and clinical settings. This compound is distinct from native GHRH in its stability profile.
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.
== Excipient == Excipient has a significant impact on the final product performance, manufacturability, and stability. Therefore, the selection of excipients has to be carefully considered during topical cream formulation design.
Some GLP-1 agonists, such as tirzepatide, are also agonists of the GIP receptor, glucagon receptor, and/or amylin receptor. These additional targets are hoped to increase the amount of weight loss the drugs cause.
The primary compounds responsible for analgesia are DHC and DHC-6-G. Although some of the metabolites are far more potent, the concentration of NDHM and NDHM-6-G in urine were minimal, suggesting no significant role in pain relief. After oral absorption, the drug is absorbed relatively rapidly with mean peak concentration at 1.7 hours. The mean half-life is 4 hours. The mean bioavailability of orally administered drug is 21%. Metabolite concentrations are high in relation to the parent drug, suggesting extensive first-pass metabolism. Dihydrocodeine tablets may possess an extended-release mechanism, lowering peak concentrations and increasing duration of action.
=== Economics === Initial pricing (AWP) is $58,000 per reversal (800 mg bolus + 960 mg infusion, $3,300 per 100 mg vial) which is higher than reversal agents for other DOAC agents (idarucizumab for use in dabigatran reversal is $4,200 per reversal).
=== Genetic diseases === Glycolytic mutations are generally rare due to importance of the metabolic pathway; the majority of occurring mutations result in an inability of the cell to respire, and therefore cause the death of the cell at an early stage. However, some mutations (glycogen storage diseases and other inborn errors of carbohydrate metabolism) are seen with one notable example being pyruvate kinase deficiency, leading to chronic hemolytic anemia. In combined malonic and methylmalonic aciduria (CMAMMA) due to ACSF3 deficiency, glycolysis is reduced by −50%, which is caused by reduced lipoylation of mitochondrial enzymes such as the pyruvate dehydrogenase complex and α-ketoglutarate dehydrogenase complex.
Sources: en.wikipedia.org
CCCP-86000 (c/n 0101) – The first prototype Il-86 is preserved at the Ukraine State Aviation Museum in Kyiv, Ukraine. It retains its original Soviet Aeroflot livery. RA-86062 (c/n 51483203029) – Preserved at the Ulyanovsk Museum of Civil Aviation in Ulyanovsk, Russia. The aircraft previously operated for Aeroflot, Belavia, and Atlant-Soyuz Airlines, and currently carries the Atlant-Soyuz livery. RA-86097 (c/n 51483207068) – Preserved as a museum aircraft at Tolmachevo Airport in Novosibirsk, Russia. It was formerly operated by S7 Airlines (Sibir Airlines) and was converted into an on-site aviation history exhibit after its retirement.
== Structure == Delta hexatoxin Hv1 is a tightly folded polypeptide that contains a chain of 42 amino acid residues and has the chemical formula C206H318N58O60S9. The amino acid sequence of delta hexatoxin Hv1 is:The tertiary structure of δ-ACTX-Hv1 contains a core β region that is made up of the residues Cys1–Cys8, Cys14–Val21, and Ser30–Ser33, with Tyr22–Gly29 protruding outwards. The β region has a three-stranded antiparallel β sheet comprising Asn6–Trp7 (β1), Met18–Val21 (β2), and Ser30–Ser33 (β3). The C-terminal end of the short β1 is held in place by a bifurcated hydrogen bond between the Cys8 amide proton and the carbonyl oxygens of the two residues preceding β strand 3 (Gln28 and Gly29). The β region also contains type II β turns at Lys3–Asn6 and Cys15–Met18 with a rare cis peptide bond at Cys16–Met 17. The nonpolar C-terminal 310 helix formed by Ile35–Lys41, bordering Lys40 and Lys41 and connecting to β region with a disulphide bond next to a β turn. The β region contains hydrophobic cysteine sidechains bordered by a lysine sidechain.Three of the four disulphide bonds form the ICK. The structure of the cystine knot motif found in versutoxin is similar to the one found in gurmarin, a 35-residue plant polypeptide used to test the inhibition of sweet taste receptors.
In zero field NMR all magnetic fields are shielded such that magnetic fields below 1 nT (nanotesla) are achieved and the nuclear precession frequencies of all nuclei are close to zero and indistinguishable. Under those circumstances the observed spectra are no-longer dictated by chemical shifts but primarily by J-coupling interactions which are independent of the external magnetic field. Since inductive detection schemes are not sensitive at very low frequencies, on the order of the J-couplings (typically between 0 and 1000 Hz), alternative detection schemes are used. Specifically, sensitive magnetometers turn out to be good detectors for zero field NMR. A zero magnetic field environment does not provide any polarization hence it is the combination of zero field NMR with hyperpolarization schemes that makes zero field NMR desirable.
== Species distribution == Steroids are present across all domains of life, including bacteria, archaea, and eukaryotes. In eukaryotes, steroids are particularly abundant in fungi, plants, and animals.
Bugs then shows Neo her crew in an abandoned theater. Morpheus, part of Bugs' group once again, offers a blue pill and a red pill to Neo, who takes the red pill. The team then "unplugs" Neo and with the help of a friendly machine, who was hacked, he is revived in the real world inside Bugs' ship, the Mnemosyne. In the real world, after Morpheus helps Neo regain his memories and fighting style, the Mnemosyne goes to Io, the last human city led by Niobe. Niobe reveals that, when Zion was nearly destroyed by the machines in another war, she and the rest of the inhabitants escaped and made a new city with the help of some machines. After sixty years, Niobe does not trust Neo, but lets the Mnemosyne crew destroy the Matrix with the help of Sati, the sentient program who helped Neo in Revolutions. In the Matrix, Neo's therapist, named the Analyst, a program designed to study the human psyche and the new leader of both the Matrix and the machines, explains that after Neo and Trinity's deaths, he was able to resurrect them to study them. He found that suppressing their memories but keeping them close to one another made the Matrix more power-efficient and more resistant to the anomalies that caused the previous iterations to fail. However, Neo's liberation destabilized the system and triggered a fail-safe to reboot the Matrix. The Analyst stalled the reboot by convincing his superiors that threatening to kill Trinity would get Neo to voluntarily return to his pod.
Sources: en.wikipedia.org
No. It is a laboratory-made analog of growth hormone-releasing hormone. The natural hormone is a 44-residue peptide, while the analog is built on a shorter 29-residue fragment.
The original material included a linker that binds serum albumin. A later variant removed that linker to reduce the duration of action. Catalogs and papers did not consistently adopt separate names, so both remain widely labeled with the same term.
The amino acid sequence and the presence or absence of the linker group. Mass measured by spectrometry gives an independent check that separates the two forms.
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.