The short version of GHRH analog fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2026-01-22 and is reviewed periodically as new material appears.
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.
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.
Batch-to-batch consistency depends on solid-phase peptide synthesis and subsequent purification. Coupling efficiency, resin choice, and cleavage conditions all affect the final profile. Counter-ion content and moisture can shift the apparent mass of a batch. Documentation typically includes a certificate of analysis with chromatograms and spectra. Independent verification by a second laboratory is sometimes requested. Whether a given certificate reflects the actual vial contents depends on chain of custody. Analytical methods themselves carry uncertainty that should be stated alongside results.
Lyophilized material is typically stored at minus twenty degrees Celsius or lower. Keeping the vial dry and protected from light preserves peptide integrity. Repeated freeze-thaw cycles can cause aggregation or loss of activity. Once dissolved, solutions are generally kept at two to eight degrees Celsius. Stability data for reconstituted solutions vary, and long-term behavior is not fully established. Working aliquots reduce the number of times a stock container is opened.
Reverse-phase high-performance liquid chromatography is the standard tool for purity assessment. The technique separates the target peptide from truncated or modified byproducts. Mass spectrometry confirms molecular weight and supports sequence verification. Electrospray ionization and matrix-assisted laser desorption are both used. Amino acid analysis provides an independent check on composition. Purity values are commonly reported as area percentage from the chromatogram. Residual trifluoroacetate and water content are also measured in many quality programs.
| Property | Value | Notes |
|---|---|---|
| Molecular weight, DAC form | About 3647 Da | Varies with salt form |
| Molecular weight, non-DAC form | About 3358 Da | MOD GRF(1-29) |
| Solubility class | Water soluble | Also dissolves in polar solvents |
| Reported half-life, DAC form | About five to eight days | Values from human studies |
| Common synonyms | CJC-1295; MOD GRF(1-29) | Name depends on variant |
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.
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.
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.
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.
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The process of photosynthesis provides the main input of free energy into the biosphere, and is one of four main ways in which radiation is important for plant life. The radiation climate within plant communities is extremely variable, in both time and space. In the early 20th century, Frederick Blackman and Gabrielle Matthaei investigated the effects of light intensity (irradiance) and temperature on the rate of carbon assimilation.
== Analogues == Several growth hormone analogues featuring amino acid substitutions, deletions, and extensions have been developed, resulting in variants with distinct pharmacokinetic and pharmacodynamic profiles.
According to the US, in 2024, China continues to be the primary supplier of chemical precursors to Mexican drug cartels, and Chinese money launderers have become central to the global drug trade. In December 2024, a Chinese national in Chicago was sentenced to 10 years in prison laundering $62 million in drug money for Mexican traffickers involving currency swaps between United States and China, and China and Mexico. In January 2025, two former executives of a Chinese chemical company were convicted of a scheme to import fentanyl precursor chemicals into the United States. One was sentenced to 25 years in prison and the other to 15 years.
Monoisotopic mass (Mmi) is one of several types of molecular masses used in mass spectrometry.The theoretical monoisotopic mass of a molecule is computed by taking the sum of the accurate masses (including mass defect) of the most abundant naturally occurring stable isotope of each atom in the molecule. It is also called the (theoretical) exact mass. This differs from the nominal molecular mass, which is the sum of the mass number of the primary isotope of each atom in the molecule and is an integer. It also is different from the molar mass or the average molecular weight, which uses the (abundance-weighted) average atomic masses. For small molecules made up of low-atomic-number elements, the monoisotopic mass is observable as a peak in a mass spectrum. For some atoms like carbon, oxygen, hydrogen, nitrogen, and sulfur, the Mmi of these elements is exactly the same as the mass of its lightest isotope. However, this does not hold true for all atoms. Iron's most common isotope has a mass number of 56, while the stable isotopes of iron vary in mass number from 54 to 58. Monoisotopic mass is typically expressed in daltons (Da).
Sources: en.wikipedia.org
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=== Transition zone: a changing microstructure === As solidification slows and growth kinetics become rate-limiting, the ice crystals begin to exclude the particles, redistributing them within the suspension. A competitive growth process develops between two crystal populations, those with their basal planes aligned with the thermal gradient (z-crystals) and those that are randomly oriented (r-crystals) giving rise to the start of the TZ. There are colonies of similarly aligned ice crystals growing throughout the suspension. There are fine lamellae of aligned z-crystals growing with their basal planes aligned with the thermal gradient. The r-crystals appear in this cross-section as platelets but in actuality, they are most similar to columnar dendritic crystals cut along a bias. Within the transition zone, the r-crystals either stop growing or turn into z-crystals that eventually become the predominant orientation, and lead to steady-state growth. There are some reasons why this occurs. For one, during freezing, the growing crystals tend to align with the temperature gradient, as this is the lowest energy configuration and thermodynamically preferential. Aligned growth, however, can mean two different things. Assuming the temperature gradient is vertical, the growing crystal will either be parallel (z-crystal) or perpendicular (r-crystal) to this gradient. A crystal that lays horizontally can still grow in line with the temperature gradient, but it will mean growing on its face rather than its edge.
The reaction is reliable and proceeds to completion. Less unreacted starting material will simplify analysis. Also, this allows a small amount of analyte to be used. The reaction is general, allowing a wide range of substrates, yet specific to a single functional group, reducing complicating interference. The products are relatively stable, and form no degradation products within a reasonable period, facilitating analysis. Some examples of good derivatization reactions are the formation of esters and amides via acyl chlorides.
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where the initial state is the acid solution with no Ca2+ (not taking into account possible CO2 dissolution) and the final state is the solution with saturated Ca2+. For strong acid concentrations, all species have a negligible concentration in the final state with respect to Ca2+ and A− so that the neutrality equation reduces approximately to 2[Ca2+] = [A−] yielding [Ca2+] ≈ 0.5 [A−]. When the concentration decreases, [HCO−3] becomes non-negligible so that the preceding expression is no longer valid. For vanishing acid concentrations, one can recover the final pH and the solubility of CaCO3 in pure water. In the case of a weak monoacid (here we take acetic acid with pKa = 4.76) with decreasing total acid concentration [A] = [A−] + [AH], we obtain:
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It is a synthetic peptide modeled on growth hormone-releasing hormone. The molecule is used in research on pituitary growth hormone secretion. It differs from the natural hormone through several stabilizing substitutions.
The DAC form carries a maleimide group that binds albumin and extends circulation time. The non-DAC form lacks this group and clears much faster. Both share the same receptor-binding core.
It targets the growth hormone-releasing hormone receptor on pituitary somatotroph cells. Activation raises cyclic AMP and promotes growth hormone release. Normal feedback pathways remain part of the response.
The powder is normally held at minus twenty degrees Celsius or below. Light and moisture exposure should be minimized. Repeated warming and cooling cycles are avoided.