Mod GRF(1-29) is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Updated 2025-11-19. Numbers and descriptions here follow the published literature rather than marketing material.
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.
Two forms circulate in research settings and are frequently confused. One carries the drug affinity complex and is often written as CJC-1295 with DAC; the other lacks that group and is usually called modified GRF(1-29). The two share the same core sequence but differ sharply in how long they persist in blood. Products labelled only as CJC-1295 normally refer to the version carrying the complex. Documentation that omits the distinction leaves the intended molecule ambiguous.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C152H252N44O42 | Cited for the form without the drug affinity complex |
| Molecular weight | About 3368 Da | Reported value for modified GRF(1-29) |
| Appearance | White to off-white powder | Lyophilised solid as usually supplied |
| Solubility | Soluble in water and polar solvents | Clarity depends on purity and salt content |
| Typical storage | -20 C or below, dry | Protect from light and repeated warming cycles |
Lyophilized material is generally stable for extended periods when held at minus twenty degrees Celsius or below and protected from moisture and light. In solution the peptide is more labile; bond hydrolysis, aggregation and oxidation of susceptible residues all proceed faster at ambient temperature. Repeated freeze and thaw cycles should be avoided because they promote clumping and loss of soluble material. The conjugated variant adds a further consideration, since the maleimide group can hydrolyze in aqueous buffer and lose its ability to react with albumin.
Laboratory handling centers on minimizing exposure to water, heat and oxygen before use. Working solutions are typically prepared in sterile water or a mild buffer, and any residual particulate matter is removed by filtration. When the powder dissolves slowly, a small proportion of acetonitrile or dilute acetic acid is sometimes added as a co-solvent. Containers are kept sealed and desiccated between uses. Records of lot number, reconstitution date and storage conditions support later comparison of results across experiments.
Identity and purity are established with reversed phase high performance liquid chromatography coupled to mass spectrometry. The chromatographic step separates the target peptide from truncated sequences and deletion products, while the mass measurement confirms the expected molecular weight to within a fraction of a dalton. Because the two common variants differ by the presence of the linker, mass alone can distinguish them in the unconjugated state. Amino acid analysis and peptide mapping are used when sequence level confirmation is required.
Two forms circulate under the CJC-1295 name, and they differ by a single appended group. The version without a drug affinity complex carries four substitutions along the peptide chain, including a D-alanine near the amino terminus and replacements at three other positions. These changes block the enzyme dipeptidyl peptidase IV and remove a methionine residue that is prone to oxidation. The modified fragment is frequently labeled MOD GRF 1-29. Naming conventions are inconsistent across informal sources, which is a common source of confusion.
The second form adds a maleimide-bearing linker to the lysine at the carboxyl end. This group reacts with cysteine-34 on circulating serum albumin, forming a covalent bond that keeps the peptide in the bloodstream for far longer. ConjuChem developed the molecule as a way to extend the action of a peptide without frequent administration. The albumin attachment is the defining structural feature of the drug affinity complex version. Whether continuous exposure produces effects distinct from shorter pulses remains an unresolved research question.
The peptide binds GHRH receptors on somatotroph cells within the anterior pituitary, triggering a signalling cascade that increases growth hormone secretion. Its improved resistance to dipeptidyl peptidase IV degradation distinguishes it from the parent hormone. In the DAC-bearing version, a maleimide group reacts with a cysteine residue on serum albumin, forming a covalent bond that keeps the peptide in circulation far longer. That albumin attachment is the central design feature separating the two research variants.
Pharmacokinetic behaviour differs sharply between the two forms. The DAC-bearing peptide shows an extended circulation time measured in days, whereas the version without the complex is cleared within roughly half an hour. This gap shapes how researchers design dosing schedules in animal models. Whether the prolonged presence of the DAC form produces effects meaningfully different from the short-acting variant remains an open question, since comparative human data are scarce.
CJC-1295 is a synthetic peptide designed to mimic growth hormone-releasing hormone (GHRH), the endogenous signal that prompts the pituitary gland to release growth hormone. The compound is a modified fragment of the natural hormone, spanning the first twenty-nine amino acids of GHRH with several substitutions that slow enzymatic breakdown. Two variants circulate in research settings: one carrying a drug affinity complex (DAC) and one without it. The DAC-free form is frequently labelled Mod GRF(1-29) in catalogs and discussion forums.
=== Aqueous phase === Rutherfordium is expected to have the electron configuration [Rn]5f14 6d2 7s2 and therefore behave as the heavier homolog of hafnium in group 4 of the periodic table. It should therefore readily form a hydrated Rf4+ ion in strong acid solution and should readily form complexes in hydrochloric acid, hydrobromic or hydrofluoric acid solutions. The most conclusive aqueous chemistry studies of rutherfordium have been performed by the Japanese team at Japan Atomic Energy Research Institute using the isotope 261mRf. Extraction experiments from hydrochloric acid solutions using isotopes of rutherfordium, hafnium, zirconium, as well as the pseudo-group 4 element thorium have proved a non-actinide behavior for rutherfordium. A comparison with its lighter homologs placed rutherfordium firmly in group 4 and indicated the formation of a hexachlororutherfordate complex in chloride solutions, in a manner similar to hafnium and zirconium.
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Sources: en.wikipedia.org
The longest known half-life of 2.2 × 1024 years of tellurium-128 was measured by the method of detecting its radiogenic daughter xenon-128; this has been used for other isotopes with noble-gas daughters and barium-130 has also been measured no other way. Another notable example is the only naturally occurring isotope of bismuth, bismuth-209, which has been predicted to be unstable with a very long half-life, but has been observed to decay. Because of their long half-lives, such isotopes are still found on Earth in various quantities, and together with the stable isotopes they are called primordial isotopes. For a list of primordial nuclides in order of half-life, see List of nuclides. 118 chemical elements are known to exist. The first 94 are found in nature, and the remainder of the discovered elements are artificially produced, with isotopes all known to be radioactive with relatively short half-lives (see below). The elements in this list are ordered according to the lifetime of their most stable isotope. Of these, three elements (bismuth, thorium, and uranium) are primordial because they have half-lives long enough to still be found on the Earth, while all the others are produced either by radioactive decay or are synthesized in laboratories and nuclear reactors. Only 13 of the 38 unstable elements have a known isotope with a half-life of at least 100 years. Every known isotope of the remaining 25 elements is highly radioactive; these are used in academic research and sometimes in industry and medicine.
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He previously worked as an analyst with the International Crisis Group.; co-founder of J Street and has served on the organization's advisory council; also a founding board member of Molad: The Center for the Renewal of Israeli Democracy as well as the Diaspora Alliance; serves on board of New Israel Fund and as trustee of Rockefeller Brothers Fund; editor with Foreign Policy magazine as editor of their Middle East Channel He publishes and speaks widely on matters related to Israel and Palestine.; has appeared on and written for The Nation, The New York Times, Ha'aretz, the BBC, Al Jazeera, and CNN. Eylon Levy (born London, 1991) is an official Israeli government spokesman, serving since the start of Gaza war. He served previously as international media advisor to President Isaac Herzog, after a career as a television news anchor at i24News and IBA News. Levy's work has appeared in Newsweek, Jerusalem Post, Times of Israel, The Daily Caller, Arutz Sheva/Israel National News, Tablet Magazine, The Washington Post, The Guardian, and The Daily Telegraph. Martin Lewis (financial journalist) (born 9 May 1972) financial journalist and broadcaster, has worked for BBC, Channel 5 (British TV channel), ITV's This Morning (TV programme) and written for The Sunday Post, The Yorkshire Post, the Manchester Evening News, Express & Star, has been a columnist for The Sunday Times, News of the World, The Guardian and the Sunday Express. Tim Lott(born 23 January 1956); author and journalist for The Guardian.
== Antimicrobial activity == Imipenem/cilastatin/relebactam has improved activity against P. aeruginosa with decreased porins expression and/or overproducing β-lactamases of the category "AmpC", thanks to relebactam AmpC inhibition. Imipenem/cilastatin/relebactam maintains a limited activity against blaOXA-48-expressing carbapenem-resistant Enterobacterales, and has no activity against metallo-β-lactamase-producing isolates. Relebactam has no activity against OXA class D β-lactamases of A. baumannii. For susceptibility testing purposes, the concentration of relebactam is fixed at 4 mg/L. The European Committee on Antimicrobial Susceptibility Testing (EUCAST) provided a susceptibility clinical breakpoint of ≤2 mg/L for Enterobacterales, P. aeruginosa, and Acinetobacter spp., while The Clinical & Laboratory Standards Institute (CLSI) provided a susceptibility clinical breakpoint of ≤1 mg/L for Enterobacterales and ≤2 mg/L for P. aeruginosa.
Sources: en.wikipedia.org
It is a synthetic peptide analogue of growth hormone-releasing hormone. Four substitutions in its sequence make it more resistant to enzymatic degradation than the natural hormone. In the version carrying a drug affinity complex, the peptide binds albumin and remains in circulation for days.
No regulatory agency has approved CJC-1295 for clinical use. Human trials were conducted in the 2000s, but the development programme was discontinued before any marketing application succeeded. Material sold today is offered as a research chemical, and its purity depends on the supplier.
Sermorelin is an unmodified fragment of growth hormone-releasing hormone and is cleared quickly. CJC-1295 contains substitutions that resist breakdown, and the form with a drug affinity complex persists much longer. Both act at the same receptor but differ substantially in duration of action.
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.