This is a working overview of GHRH analog, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2026-07-17 and is reviewed periodically as new material appears.
CJC-1295 belongs to a family of synthetic peptides modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. The compound is built from the first twenty-nine amino acids of the natural human sequence, a fragment that retains full receptor binding capacity. Native growth hormone-releasing hormone is degraded quickly in circulation, so the fragment alone has limited practical value. Early work therefore focused on chemical modifications that preserve receptor binding while slowing enzymatic breakdown. The result is a molecule described in the literature as a long-acting analog of the natural hormone.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular weight (no linker) | ~3.37 kDa | Calculated from peptide sequence |
| Molecular weight (with linker) | ~3.65 kDa | Includes albumin-binding moiety |
| Appearance | White to off-white powder | Typically lyophilized |
| Solubility | Soluble in water | Also dissolves in aqueous buffers |
| Common synonyms | Modified GRF(1-29), DAC:GRF | Usage varies by source |
Lyophilised powder is the usual supplied form. The material is hygroscopic, so vials are typically equilibrated to room temperature before opening in order to prevent condensation on the contents. Long-term storage is generally described at minus twenty degrees Celsius or colder, protected from light and moisture. Repeated freeze-thaw cycles are avoided because they promote aggregation and loss of soluble material. A reconstituted solution is considerably less stable than the dry powder and is normally kept refrigerated for short periods only.
Identity and purity are assessed mainly by reversed-phase high-performance liquid chromatography combined with mass spectrometry. The chromatographic separation resolves the target peptide from truncation products and from species carrying oxidised residues, while mass measurement confirms the expected molecular mass. Because the two common variants differ by roughly 280 daltons, a mass determination distinguishes them unambiguously. Purity is often quoted as a percentage of total peak area, although that figure depends on the detection wavelength and the integration method applied.
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.
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 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.
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.
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.
CJC-1295 acts at the growth hormone-releasing hormone receptor, a G-protein-coupled receptor found on somatotroph cells in the anterior pituitary. Binding triggers a rise in cyclic AMP and calcium entry, which promotes release of stored growth hormone. Because the peptide mimics the body's own releasing hormone, it amplifies existing secretory pulses rather than driving continuous output. The size of the response therefore depends partly on the subject's own hormonal rhythm and feedback state.
Dulgo pole Zefir Bulgarian population #2 Clone 11-6-22 Clone 80-121-33 Mitcham Digne 38 Mitcham Ribecourt 19 'Todd's Mitcham', a verticillium wilt-resistant cultivar produced from a breeding and test program of atomic gardening at Brookhaven National Laboratory from the mid-1950s 'Refined Murray', also verticillium-resistant 'Roberts Mitcham', also verticillium-resistant and also the product of mutation breeding
The Ebers Papyrus is among the oldest and most important medical papyri of Ancient Egypt. Written c. 1550 BC, it was likely copied from a series of much earlier texts, and contains a passage from the First Dynasty (c. 3400 BC). The document is named after Georg Ebers, who purchased the document in 1872 in the city of Luxor, the site of Thebes (known to Ancient Egyptians as Waset). Thebes was the most venerated city of Ancient Egypt in its heyday during the Middle Kingdom and New Kingdom. The Ebers Papyrus is thought to contain the first known medical reference to diabetes, by the phrase: "...to eliminate urine which is too asha". The crucial word asha can mean both "plentiful" and "often". It is unclear whether the condition described was excessive urine (polyuria), which may have been symptomatic of diabetes, or increased frequency of urine, very often due to urinary tract infection. The following mixture was prescribed for treatment: "A measuring glass filled with Water from the Bird pond, Elderberry, Fibres of the asit plant, Fresh Milk, Beer-Swill, Flower of the Cucumber, and Green Dates". Urinary troubles in the adult were also corrected with "rectal injections of olive oil, honey, sweet beer, sea salt, and seeds of the wonderfruit".
All human remains at the site were found to contain "very high levels" of mercury. This is believed to be either due to their continuous exposure to mercury-containing cinnabar or because their skin was painted with mercury. Additionally, evidence of osteoarthritis was found in bones, which may indicate that those humans either walked a lot or were dancers.
Sources: en.wikipedia.org
== Biography == Macleod was born in Clunie, near Dunkeld in Perthshire. Soon after he was born, his father Robert Macleod, a minister of the Free Church, was transferred to Aberdeen, where John attended Aberdeen Grammar School and enrolled in the study of medicine at the University of Aberdeen. At the University of Aberdeen, one of MacLeod's principal teachers was the young professor John Alexander MacWilliam. He was awarded his medical degree with honours in 1898 and then spent a year studying biochemistry at the University of Leipzig, Germany, on a travelling scholarship. He became a demonstrator at the London Hospital Medical School, where in 1902 he was appointed lecturer in biochemistry. In the same year, he was awarded a doctorate in public health from Cambridge University. Around that time he published his first research article, a paper on phosphorus content in muscles. In 1903, Macleod became a lecturer in physiology at the Western Reserve University in Cleveland, Ohio, where he remained for 15 years. This was the period when he developed an interest in carbohydrate metabolism that was to last for the rest of his career. In 1910, he delivered a lecture on various forms of experimental diabetes and their significance for diabetes mellitus at the joint meeting of the section on Pharmacology and Therapeutics and the section on Pathology and Physiology of the American Medical Association. In 1916, he was a Professor of Physiology at McGill University in Montreal, Canada.
=== Hormones === Since Sjögren's disease has a higher prevalence in women, sex hormones, especially estrogen, are believed to affect humoral and cell-mediated immune responses, influencing susceptibility to the disease. Androgens are generally considered to prevent autoimmunity. Studies on mice models suggest estrogen deficiency stimulates presentation of autoantigens, inducing Sjögren's-like symptoms.
Phosphotungstic acid haematoxylin (PTAH) is a mix of haematoxylin with phosphotungstic acid, used in histology for staining. It stains some tissue in contrasting colors in a way similar to haematoxylin and eosin stain, as phosphotungstic acid binds to tissue proteins. It is used to show gliosis in the central nervous system, tumours of skeletal muscles, and fibrin deposits in lesions. Muscle is stained blue-black to dark brown, connective tissue is pale orange-pink to brownish red, fibrin and neuroglia stain deep blue, coarse elastic fibers show as purple, and bone and cartilage obtain yellowish to brownish red color. PTAH is ideal for demonstrating striated muscle fibers and mitochondria, often without a counterstain. As such, it is used to identify contraction bands, as seen in contraction band necrosis. PTAH can be helpful in diagnosing oncocytomas, infantile digital fibromas. PTAH stains ependymomas while it does not stain choroid plexus papillomas, providing one means of differentiating these tumors. This technique has been largely replaced by immunohistochemistry techniques.
Sources: en.wikipedia.org
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.
Early development used the albumin-binding form, and a shorter variant was later discussed under the same label. Because the two differ in half-life and handling, ambiguity arises whenever a source omits the variant designation.
The compound derives from that fragment but is not identical to it. The parent fragment lacks the stabilizing substitutions, so its degradation rate and duration of action differ noticeably.
Chromatography reports how much material elutes as a single peak but does not confirm what that material is. Mass spectrometry supplies the molecular mass, which is characteristic of a given sequence and its modifications. Together the two methods support both a purity figure and an identity claim.