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.
Last reviewed on 2026-03-27. Where a claim depends on a specific study, the study is described rather than over-claimed.
Binding to GHRH receptors on pituitary somatotroph cells triggers cyclic AMP signaling and stimulates growth hormone synthesis and release. Because the peptide acts upstream of the pituitary, effects are mediated through endogenous growth hormone rather than direct receptor activation in peripheral tissues. Increases in insulin-like growth factor 1 are generally described as a downstream consequence. Most published human exposure data come from small early-stage studies, and the clinical significance of the pharmacokinetic profile remains incompletely characterized.
CJC-1295 is a synthetic analogue of growth hormone-releasing hormone, built on the 29-amino-acid GHRH(1-29) fragment. Four substitutions distinguish it from the natural sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27. These changes reduce enzymatic cleavage and extend the peptide's persistence in circulation. The compound is discussed in two forms, one carrying a drug affinity complex and one without it.
The drug affinity complex is a maleimidopropionic acid group attached to a lysine side chain. It reacts with the free thiol of cysteine-34 on circulating albumin, forming a covalent bond. This conjugation keeps the peptide in the bloodstream and shields it from rapid renal filtration and proteolysis. Reported circulation half-lives for the albumin-bound form fall in the range of roughly six to nine days in early human studies.
Two related forms appear under the CJC-1295 name. The simpler analogue, commonly written as modified GRF(1-29), carries the four substitutions but no additional conjugation. The second form attaches a maleimidopropionic acid linker to a lysine residue, a modification frequently called the drug affinity complex. That linker reacts with the free thiol on serum albumin to form a covalent bond. Because albumin has a long residence time in blood, the conjugated peptide stays in circulation far longer than the unconjugated analogue.
Receptor level activity follows the canonical GHRH pathway. The peptide binds the GHRH receptor, a class B G protein coupled receptor on somatotroph cells of the anterior pituitary. Binding raises intracellular cyclic AMP, which promotes calcium entry and the release of growth hormone into the bloodstream. Because the molecule acts at the same receptor as the endogenous hormone, its effect is superimposed on the natural pulsatile rhythm rather than replacing it. Whether sustained receptor occupation leads to desensitization is not fully settled.
| Property | Value | Notes |
|---|---|---|
| Physical form | Lyophilized white powder | Supplied as a freeze-dried solid for research use |
| Molecular weight | Approximately 3,647 Da (DAC form) | Lower for the variant lacking the albumin-binding moiety |
| Solubility | Soluble in water and aqueous buffer | Typically dissolved in sterile or bacteriostatic water |
| Typical storage temperature | −20 °C or below | Dry powder, desiccated and protected from light |
| Common analytical method | Reversed-phase HPLC with mass spectrometry | Used for purity estimation and identity confirmation |
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.
The attached maleimide group explains the unusual duration of the DAC version. After injection it reacts with the thiol of cysteine-34 on serum albumin, forming a stable covalent bond. The resulting conjugate is too large for rapid kidney filtration and is shielded from many peptidases. Reported half-lives for this form reach several days, whereas the version without the group is cleared in roughly half an hour. That gap is the main pharmacological difference between the two.
Downstream of growth hormone, the liver and other tissues increase production of insulin-like growth factor 1, a mediator of many growth-promoting effects. Studies have documented elevated levels of both hormones after dosing, and the rise from the long-acting form persists longer than that produced by shorter-acting analogues. What remains unclear is whether sustained elevation of these markers translates into meaningful clinical benefit, and whether prolonged exposure carries risks that short trials could not detect.
== Partnerships == The company entered into a co-marketing and sales agreement with Thermo Fisher Scientific in November 2024 to promote the integration of Seer’s Proteograph system with Thermo Fisher’s Orbitrap mass spectrometers. In June 2025, Seer announced a collaboration with Korea University and major Korean cancer centers, including Seoul National University Hospital and Samsung Medical Center. The partnership will support a large-scale plasma proteomics study aimed at identifying blood-based biomarkers for cancers in young adults. The study will utilize Seer’s Proteograph platform and a mass spectrometer from Thermo Fisher Scientific to analyze over 20,000 plasma samples.
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The NIH Office of the Director is the central office responsible for setting policy for the NIH, and for planning, managing, and coordinating the programs and activities of all NIH components. The NIH Director plays an active role in shaping the agency's activities and outlook. The Director is responsible for providing leadership to the Institutes and Centers by identifying needs and opportunities, especially in efforts involving multiple Institutes. Within the Director's Office is the Division of Program Coordination, Planning and Strategic Initiatives with 12 divisions including:
Sources: en.wikipedia.org
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The main SF unit in South Vietnam was the 5th Special Forces Group (Airborne). SF soldiers assigned to the 5th Group earned sixteen Medals of Honor in Vietnam, making it the most prominently decorated unit for its size in that conflict. The unit was also awarded the coveted Presidential Unit Citation for extraordinary heroism during the Vietnam War from 1 November 1966 – 31 January 1968. Army Special Forces personnel also played predominant roles in the highly secret, covert, multi-service Military Assistance Command Vietnam Studies and Observation Group (MACV-SOG), with an extraordinarily large number of covert U.S. military personnel killed or lost MIA while operating on Studies and Observations Group (SOG) reconnaissance missions in Laos and Cambodia. During the prolonged conflict the Army Special Forces trained regular and paramilitary units of several Allied nations as well as US reconnaissance members; supervised the indigenous Civilian Irregular Defense Group stationed throughout Vietnam in fortified camps and as backup reserves; monitored the border region and infiltration routes; conducted strategic intelligence missions and fielded numerous elements engaged in special operational tasks. From 1957 to 1973, over 20,000 Special Forces soldiers served out of a total of 3.2 million American servicemen, who were deployed throughout the war. Of these 882 died, killed in action or went missing in Southeast Asia (including 121 in Laos and 32 in Cambodia). The "Green Beret Affair": U. S.
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Sources: en.wikipedia.org
The two share the same 29-amino-acid backbone. CJC-1295 carries an additional albumin-binding moiety that markedly extends its residence time in circulation, while the form without that moiety clears faster. Literature sometimes applies the name loosely to either variant.
It has not been approved by major regulatory agencies for any therapeutic indication. Material sold under this name is typically distributed for laboratory research only. Clinical use is not supported by large controlled trials.
Early human studies of the albumin-binding form reported circulation half-lives on the order of several days. The value depends on assay method and study design. Estimates for the form without the binding moiety are considerably shorter.
The names are often used interchangeably in casual writing, but they are not strictly identical. Modified GRF(1-29) refers to the unconjugated analogue carrying only the four substitutions. The version sold as CJC-1295 with DAC includes the albumin binding linker and clears much more slowly.