If you have been reading about DAC group 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 2025-08-02. Numbers and descriptions here follow the published literature rather than marketing material.
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.
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.
CJC-1295 belongs to a class of synthetic peptides modeled on growth hormone releasing hormone, a forty-four amino acid signal produced by the hypothalamus. The compound is built from the first twenty-nine residues of the natural sequence, with four substitutions introduced at positions 2, 8, 15 and 27. These changes were designed to slow enzymatic breakdown while preserving receptor activation. The result is a peptide that is shorter than native GHRH and considerably more resistant to ordinary clearance pathways in circulation.
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 |
|---|---|---|
| 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 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.
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.
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.
Ciramadol (WY-15,705) is an opioid analgesic that was developed in the late 1970s and is related to phencyclidine, tramadol, tapentadol and venlafaxine. It is a mixed agonist-antagonist for the μ-opioid receptor with relatively low abuse potential and a ceiling on respiratory depression which makes it a relatively safe drug. It has a slightly higher potency and effectiveness as an analgesic than codeine, but is weaker than morphine. Other side effects include sedation and nausea but these are generally less severe than with other similar drugs.
Chains shoots and kills Nancy, then straps a bomb to Joe's chest and has him tied up in a helicopter on its way to the Capitol. Joe escapes and seizes control of the helicopter. Inside of the courtroom, Chains retrieves a hidden submachine gun and uses it to kill government agent Martinez, two security officers, all of the justices and Whipperton. Joe overpowers Chains and hands him over to the authorities. Chains frees himself and steals a revolver from an officer, aiming for Joe. Lance intervenes and shoots Chains twice, sending him tumbling over a railing to his death. Joe exits the courthouse as SWAT officers storm the building.
== Structure == TRAIL shows homology to other members of the tumor necrosis factor superfamily. It is composed of 281 amino acids and has characteristics of a type II transmembrane protein. The N-terminal cytoplasmic domain is not conserved across family members, however, the C-terminal extracellular domain is conserved and can be proteolytically cleaved from the cell surface. TRAIL forms a homotrimer that binds three receptor molecules.
Sources: en.wikipedia.org
The influence of Nasser's Arab nationalism over the RCC was immediately apparent. The administration was instantly recognized by the neighbouring Arab nationalist regimes in Egypt, Syria, Iraq, and Sudan, with Egypt sending experts to aid the inexperienced RCC. Gaddafi propounded pan-Arab ideas, proclaiming the need for a single Arab state stretching across North Africa and the Middle East. In December 1969, Libya signed the Tripoli Charter alongside Egypt and Sudan. This established the Arab Revolutionary Front, a pan-national union designed as a first step towards the eventual political unification of the three nations. In 1970 Syria declared its intention to join. Nasser died unexpectedly in September 1970, with Gaddafi playing a prominent role at his funeral. Nasser was succeeded by Anwar Sadat, who replaced the idea of a unified state with a political federation, implemented in April 1971; in doing so, Egypt, Syria, and Sudan received large grants of Libyan oil money. In July 1971, Gaddafi sided with Sadat against the Soviet Union in the 1971 Sudanese coup d'état and dispatched Libyan fighter jets to force down a British Overseas Airways Corporation jetliner carrying the leading coup plotters, Farouk Osman Hamadallah and Babikir al-Nour. They were extradited back to Khartoum, where they were promptly executed by Sudanese leader Jaafar Nimeiry. In February 1972, Gaddafi and Sadat signed an unofficial charter of merger, but it was never implemented because relations broke down the next year.
== Awards and recognition == 1997: Newcomb Cleveland Prize 1998: W. Alden Spencer Award 1999: Albert Lasker Basic Medical Research Award 2000: Rosenstiel Award 2001: Gairdner Foundation International Award 2003: Louisa Gross Horwitz Prize 2003: Nobel Prize in Chemistry
=== Plasma ACTH concentration === This test may also be referred to as a ‘’resting ACTH’’, ’’endogenous ACTH’’, or ‘’basal ACTH’’. The majority of ACTH produced in normal horses comes from corticotrope cells in the pars distalis, with only 2% thought to come from melanotropes in the pars intermedia. In horses with PPID, melanotropes produce abnormally high concentrations of ACTH. Basal plasma ACTH concentrations, which measure the blood levels of circulating ACTH, can therefore be useful in diagnosing the disease. ACTH levels naturally fluctuate in healthy horses, with a significant rise occurring the in autumn (August through October) in North American horses. Horses with PPID have a similar, but much more significant, rise in the autumn. Therefore, a seasonally adjusted reference range must be used that correlates with the time of year the sample is taken. Failure to use a seasonally adjusted reference range may lead to false-positive results in normal horses if they are sampled in the fall. Autumnal testing was thought to be more sensitive and specific than testing at other times of the year; however, this concept has been recently challenged. Basal plasma ACTH levels may increase if the horse is severely ill or under great stress or pain, such as if it has laminitis. However, such events must be fairly significant to confound the results. Additionally, ACTH levels may not be significantly increased early on in the disease, leading to false negatives.
The main role of the tissue factor (TF) pathway is to generate a "thrombin burst", a process by which thrombin, the most important constituent of the coagulation cascade in terms of its feedback activation roles, is released very rapidly. FVIIa circulates in a higher amount than any other activated coagulation factor. The process includes the following steps:
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.
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.