This is a working overview of GHRH analog, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2026-07-23. Anything still debated is marked as such rather than presented as settled.
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.
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 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.
| 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 |
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.
Lyophilized peptide powder is comparatively stable when kept dry, cold, and protected from light. Once dissolved, the molecule is vulnerable to deamidation, oxidation, and aggregation, with the rate depending on pH, buffer composition, and temperature. Alkaline conditions and repeated freeze-thaw cycles accelerate loss of the intact peptide. The methionine present in the native sequence is a known oxidation site, which is one reason it was replaced in the modified fragment. Suppliers typically recommend cold storage of solutions and use within a short window.
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.
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.
CJC-1295 is a synthetic peptide modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. Its sequence corresponds to the first twenty-nine residues of human GHRH, with four substitutions that slow enzymatic breakdown. Early descriptions placed the compound in research on growth hormone deficiency and related conditions, and later literature groups it with the long-acting GHRH analogs. The name appears in both laboratory and popular fitness writing, where it sometimes labels chemically different peptides.
Two related peptides circulate under the CJC-1295 label, and they differ mainly in how long they persist in circulation. The version carrying a drug affinity complex includes a maleimidopropionic acid linker that forms a covalent bond with serum albumin. The other version, usually written as modified GRF(1-29) or tetrasubstituted GRF(1-29), lacks that linker and is cleared quickly. Mixing the two produces inconsistent readings of published half-life values, because the linker rather than the receptor-facing sequence drives most of the difference.
The core sequence keeps the receptor-binding region of GHRH while replacing four positions that are vulnerable to dipeptidyl peptidase-4 and other proteases. Substitutions at positions 2, 8, 15, and 27 raise metabolic stability relative to the natural hormone. The N-terminal residues remain essential for activity, so changes there generally lower potency. Molecular weight sits near 3368 daltons for the tetrasubstituted analog without the linker, while the albumin-binding form is heavier because of the added maleimide group.
Purity is most often assessed by reversed-phase high-performance liquid chromatography, reported as a percentage of total peak area. Identity is confirmed by mass spectrometry, which yields a molecular ion consistent with the expected sequence. Amino acid analysis and peptide mapping provide additional characterization. Reported purity values are method-dependent, so figures from different laboratories are not always directly comparable without details of column, gradient, and detection wavelength.
Peptide degradation proceeds mainly through hydrolysis, oxidation of methionine, and deamidation of asparagine or glutamine residues. The maleimide group on the albumin-binding variant can also react with thiols or hydrolyze in aqueous media. Because these pathways accelerate with temperature and pH extremes, handling conditions strongly influence measured stability. Stability data in the public literature are limited and often generated under differing conditions, so general statements about shelf life should be read as approximate.
Research material is normally supplied as a freeze-dried powder in sealed vials. In that state the peptide is comparatively robust, but prolonged exposure to warmth, moisture, or light accelerates degradation. Storage at minus twenty degrees Celsius or lower, with desiccant and protection from light, is the commonly described practice. Vials should be allowed to reach room temperature before opening to limit condensation on the powder. Moisture uptake during handling is a recognized source of variability in later measurements.
==== MeSH D12.125.119 – amino acids, dicarboxylic ==== MeSH D12.125.119.075 – 2-aminoadipic acid MeSH D12.125.119.170 – aspartic acid MeSH D12.125.119.170.150 – d-aspartic acid MeSH D12.125.119.170.275 – isoaspartic acid MeSH D12.125.119.170.400 – n-methylaspartate MeSH D12.125.119.170.700 – potassium magnesium aspartate MeSH D12.125.119.270 – carbocysteine MeSH D12.125.119.307 – cystathionine MeSH D12.125.119.369 – cystine MeSH D12.125.119.450 – glutamic acid MeSH D12.125.119.450.150 – 1-carboxyglutamic acid MeSH D12.125.119.450.400 – glutamates MeSH D12.125.119.450.400.700 – polyglutamic acid MeSH D12.125.119.450.400.800 – sodium glutamate MeSH D12.125.119.658 – homocystine
==== ASTA pungency unit ==== The ASTA (American Spice Trade Association) pungency unit is based on a scientific method of measuring chili pepper "heat". The technique utilizes high-performance liquid chromatography to identify and measure the concentrations of the various compounds that produce a heat sensation. Scoville units are roughly 1⁄15 the size of pungency units while measuring capsaicin, so a rough conversion is to multiply pungency by 15 to obtain Scoville heat units.
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== Description == The cap of this mushroom grows up to 8–30 cm (3–12 in) wide, sometimes more. Viscid when moist, the cap is convex when young and flattens with age. The colour is generally reddish-brown, sometimes with a paler margin. The stipe grows up to 8–25 cm (3–10 in) tall and 2–7 cm (1–3 in) thick—rather large in comparison to the cap. The stem is usually enlarged at the base when young, becoming more cylindrical in age. It is finely reticulate on the upper portion or sometimes the whole. The flesh of the stem is sometimes dark yellow near the base. The undersurface of the cap consists of thin tubes, the site of spore production; they are 1 to 2 cm (1⁄2 to 3⁄4 in) deep, and whitish in colour when young, but mature to a greenish-yellow. The angular pores, which do not stain when bruised, are small—roughly 2 to 3 pores per millimetre. In youth, the pores are white and appear as if stuffed with cotton (which are actually mycelia); as they age, they change colour to yellow and later to brown. The spore print is olive brown. The flesh of the fruit body is white, thick and firm when young, but becomes somewhat spongy with age. When bruised or cut, it either does not change colour, or turns a very light brown or light red. Mature specimens can weigh about 1 kg (2 lb 3 oz). A huge specimen collected on the Isle of Skye, Scotland, in 1995 weighed 3.2 kg (7 lb 1 oz); its cap was 42 cm (16+1⁄2 in) wide and the stipe was 18 cm (7 in) tall and 14 cm (5+1⁄2 in) wide. A similarly sized specimen found in Poland in 2013 made international news.
Sources: en.wikipedia.org
In epigenetics, proline isomerization is the effect that cis-trans isomerization of the amino acid proline has on the regulation of gene expression. Similar to aspartic acid, the amino acid proline has the rare property of being able to occupy both cis and trans isomers of its prolyl peptide bonds with ease. Peptidyl-prolyl isomerase, or PPIase, is an enzyme very commonly associated with proline isomerization due to their ability to catalyze the isomerization of prolines. PPIases are present in three types: cyclophilins, FK506-binding proteins, and the parvulins. PPIase enzymes catalyze the transition of proline between cis and trans isomers and are essential to the numerous biological functions controlled and affected by prolyl isomerization (i.e. cell signalling, protein folding, and epigenetic modifications) Without PPIases, prolyl peptide bonds will slowly switch between cis and trans isomers, a process that can lock proteins in a nonnative structure that can affect render the protein temporarily ineffective. Although this switch can occur on its own, PPIases are responsible for most isomerization of prolyl peptide bonds. The specific amino acid that precedes the prolyl peptide bond also can have an effect on which conformation the bond assumes. For instance, when an aromatic amino acid is bonded to a proline the bond is more favorable to the cis conformation. Cyclophilin A uses an "electrostatic handle" to pull proline into cis and trans formations.
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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 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.