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Identity And Naming History — Reference Sheet

By Editorial Desk · published 2026-05-20 · last reviewed 2026-06-25 · Faq

GRF(1-29) comes up often in conversation and rarely with the context attached. Here we lay out the basics in order, then work through the practical considerations.

Updated 2026-06-25. 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.

Receptor Action and Clearance

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.

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

Persistence, Stability and Measurement

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.

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.

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Mechanism and Pharmacokinetics

Binding of the peptide to the growth hormone-releasing hormone receptor on pituitary somatotrophs triggers a G protein coupled cascade that raises cyclic AMP and opens calcium channels. The result is greater secretion of growth hormone into the bloodstream. Because the peptide acts at the same receptor as the natural hypothalamic hormone, its effect is amplified pulse size rather than an entirely separate release pathway. Receptor binding alone does not determine the response, since somatostatin tone and other inputs modulate the final output.

The albumin-binding version stays in circulation for days, because covalent attachment to serum albumin shields the peptide from rapid filtration and degradation. Reported half-lives for this form fall in the range of several days. The version without the linker is cleared in minutes, with estimates often near thirty minutes in animal work. These figures come from small studies and vary with assay method, species, and route, so they are best read as approximate rather than fixed constants.

Studies in this area generally track growth hormone pulses, insulin-like growth factor 1 concentrations, and occasionally body composition endpoints. Most published human data come from early, small trials, and questions about long-term effects remain open. Whether repeated exposure alters pituitary responsiveness over time is not settled. Analytical work relies on immunoassays for the hormones and on mass spectrometry for the peptide itself, because the two measurements answer different questions.

Background and Naming Conventions

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.

Background and Molecular Design

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.

Further detail

In more severe cases, the diagnosis may be able to be done via ultrasound, especially if OI is already a possibility. An ethical concern with prenatal screening for OI often arises when parents inquire as to how severely affected their child will be—such questions are as yet difficult to answer conclusively. If a non-affected person has already had a child with OI, there is a greater likelihood (although still quite remote) that their future children will have OI due to genetic mosaicism. The disability rights critique of prenatal screening for OI, held by some bioethicists and some affected individuals, negatively compares it to eugenics, with even those not opposed to abortion opposing selective abortions on the ethical ground that their existence betrays the belief that the lives of those with OI are "less worth living [and] less valuable".

Fibrils (from Latin fibra) are structural biological materials found in nearly all living organisms. Not to be confused with fibers or filaments, fibrils tend to have diameters ranging from 10 to 100 nanometers (whereas fibers are micro to milli-scale structures and filaments have diameters approximately 10–50 nanometers in size). Fibrils are not usually found alone but rather are parts of greater hierarchical structures commonly found in biological systems. Due to the prevalence of fibrils in biological systems, their study is of great importance in the fields of microbiology, biomechanics, and materials science.

=== Laminin === Laminins are proteins found in the basal laminae of virtually all animals. Rather than forming collagen-like fibers, laminins form networks of web-like structures that resist tensile forces in the basal lamina. They also assist in cell adhesion. Laminins bind other ECM components such as collagens and nidogens.

== Structure == Glycine, proline, and hydroxyproline must be in their designated positions with the correct configuration. For example, hydroxyproline in the Y position increases the thermal stability of the triple helix, but not when it is located in the X position. The thermal stabilization is also hindered when the hydroxyl group has the wrong configuration. Due to the high abundance of glycine and proline contents, collagen fails to form a regular α-helix and β-sheet structure. Three left-handed helical strands twist to form a right-handed triple helix. A collagen triple helix has 3.3 residues per turn. Each of the three chains is stabilized by the steric repulsion due to the pyrrolidine rings of proline and hydroxyproline residues. The pyrrolidine rings keep out of each other's way when the polypeptide chain assumes this extended helical form, which is much more open than the tightly coiled form of the alpha helix. The three chains are hydrogen bonded to each other. The hydrogen bond donors are the peptide NH groups of glycine residues. The hydrogen bond acceptors are the CO groups of residues on the other chains. The OH group of hydroxyproline does not participate in hydrogen bonding but stabilises the trans isomer of proline by stereoelectronic effects, therefore stabilizing the entire triple helix. The rise of the collagen helix (superhelix) is 2.9 Å (0.29 nm) per residue. The center of the collagen triple helix is very small and hydrophobic, and every third residue of the helix must have contact with the center.

Sources: en.wikipedia.org

Background from the literature

Phenformin is an antidiabetic drug from the biguanide class. It was marketed as DBI by Ciba-Geigy, but was withdrawn from most markets in the late 1970s due to a high risk of lactic acidosis, which was fatal in 50% of cases. Phenformin was developed in 1957 by Ungar, Freedman and Seymour Shapiro, working for the U.S. Vitamin Corporation. Clinical trials begun in 1958 showed it to be effective, but with gastrointestinal side effects.

=== Amino acid sequence === The linear amino acid sequence of a protein is called the primary structure. The primary structure can be easily determined from the sequence of codons on the DNA gene that codes for it. In most proteins, the primary structure uniquely determines the 3-dimensional structure of a protein in its native environment. An exception is the misfolded prion protein involved in bovine spongiform encephalopathy. This structure is linked to the function of the protein. Additional structural information includes the secondary, tertiary and quaternary structure. A viable general solution to the prediction of the function of a protein remains an open problem. Most efforts have so far been directed towards heuristics that work most of the time.

On 10 January 1972, an ad hoc strike committee led by Johannes Nangutuuala, was formed to negotiate with the South African government; the strikers demanded an end to contract labour, freedom to apply for jobs according to skill and interest and to quit a job if so desired, freedom to have a worker bring his family with him from Ovamboland while taking a job elsewhere, and for equal pay with white workers. The strike was later brought to an end after the South African government agreed to several concessions which were endorsed by Nangutuuala, including the implementation of uniform working hours and allowing workers to change jobs. Responsibility for labour recruitment was also transferred to the tribal authorities in Ovamboland. Thousands of the sacked Ovambo workers remained dissatisfied with these terms and refused to return to work. They attacked tribal headmen, vandalised stock control posts and government offices, and tore down about a hundred kilometres of fencing along the border, which they claimed obstructed itinerant Ovambos from grazing their cattle freely. The unrest also fueled discontent among Kwanyama-speaking Ovambos in Angola, who destroyed cattle vaccination stations and schools and attacked four border posts, killing and injuring some SADF personnel as well as members of a Portuguese militia unit. South Africa responded by declaring a state of emergency in Ovamboland on 4 February.

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.

Which receptor does the compound target?

It acts on the growth hormone-releasing hormone receptor found on pituitary somatotroph cells. Activation of that receptor triggers growth hormone release through a cyclic AMP dependent pathway.

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