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Identity And Naming History — What the Evidence Shows

By Editorial Desk · published 2026-01-31 · last reviewed 2026-03-09 · Data

If you have been reading about IGF-1 and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.

Updated 2026-03-09. Numbers and descriptions here follow the published literature rather than marketing material.

Identity and Naming History

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.

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.

Molecular Background and Naming

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 at a glance

PropertyValueNotes
Molecular classSynthetic peptideGHRH analog, not a steroid
Backbone length29 amino acidsBased on GRF(1-29)
SubstitutionsFour positionsD-Ala2, Gln8, Ala15, Leu27
AppearanceWhite to off-white powderTypical lyophilized research material
Common synonymsModified GRF(1-29)Usage varies between sources

CJC-1295 Background and Mechanism

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.

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.

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Receptor Action and Clearance

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.

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.

Background from the literature

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Moriarty, Philip. "Au – Gold Nanoparticle". Sixty Symbols. Brady Haran for the University of Nottingham. Point-by-point methods for citrate synthesis and hydroquinone synthesis of gold nanoparticles are available here.

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Sources: en.wikipedia.org

Reference notes

Following the deaths of children in China from powdered milk in 2008, the Joint Research Centre (JRC) of the European Commission in Belgium set up a website about methods to detect melamine. In May 2009, the JRC published the results of a study that benchmarked the ability of labs around the world to accurately measure melamine in food. The study concluded that the majority of labs can effectively detect melamine in food. In October 2008, the U.S. Food and Drug Administration (FDA) issued new methods for the analysis of melamine and cyanuric acid in infant formulations in the Laboratory Information Bulletin No 4421. Similar recommendations have been issued by other authorities, like the Japanese Ministry of Health, Labor and Welfare, both based on liquid chromatography – mass spectrometry (LC/MS) detection after hydrophilic interaction liquid chromatography (HILIC) separation. The existing methods for melamine determination using a triple quadrupole liquid chromatography – mass spectrometry (LC/MS) after solid phase extraction (SPE) are often complex and time-consuming. However, electrospray ionization methods coupled with mass spectrometry allow a rapid and direct analysis of samples with complex matrices: the native liquid samples are directly ionized under ambient conditions in their original solution. In December 2008, two new fast and inexpensive methods for detecting melamine in liquids have been published.

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Sources: en.wikipedia.org

Reference notes

This results in the Fe2+ ion switching to a low-spin configuration, resulting in a 20% decrease in ionic radius so that now it can fit into the porphyrin ring, which becomes planar. (Additionally, this hydrogen bonding results in the tilting of the oxygen molecule, resulting in a Fe–O–O bond angle of around 120° that avoids the formation of Fe–O–Fe or Fe–O2–Fe bridges that would lead to electron transfer, the oxidation of Fe2+ to Fe3+, and the destruction of hemoglobin.) This results in a movement of all the protein chains that leads to the other subunits of hemoglobin changing shape to a form with larger oxygen affinity. Thus, when deoxyhemoglobin takes up oxygen, its affinity for more oxygen increases, and vice versa. Myoglobin, on the other hand, contains only one heme group and hence this cooperative effect cannot occur. Thus, while hemoglobin is almost saturated with oxygen in the high partial pressures of oxygen found in the lungs, its affinity for oxygen is much lower than that of myoglobin, which oxygenates even at low partial pressures of oxygen found in muscle tissue. As described by the Bohr effect (named after Christian Bohr, the father of Niels Bohr), the oxygen affinity of hemoglobin diminishes in the presence of carbon dioxide.

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Sources: en.wikipedia.org

Frequently asked questions

Is this compound a naturally occurring hormone?

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.

Why do two versions share one name?

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.

What is the most reliable identifier?

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.

Is CJC-1295 a natural hormone?

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.

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