This is a working overview of Mod GRF(1-29), written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2025-07-20 and is reviewed periodically as new material appears.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Primary target | GHRH receptor | Present on pituitary somatotroph cells |
| Signal pathway | Gs, cyclic AMP, protein kinase A | Sequence follows receptor activation |
| Main measured effect | Growth hormone release | Insulin-like growth factor 1 shifts indirectly |
| Half-life, binding form | Several days | Extended through serum albumin association |
| Half-life, unmodified form | About 30 minutes | Limited mainly by enzymatic cleavage |
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.
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.
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.
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.
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== Etymology == In Old English, an alcoholic beverage made from apples was simply called æppelwīn ("apple wine"). The word cider is first mentioned in Middle English in biblical use as sicer, ciser ("strong drink", "strong liquor") in the 13th century and as sither(e) / cidre "liquor made from the juice of fruits" → "beverage made from apples" in the 14th century. It was probably first borrowed from Old French primitive form sizre "fermented beverage" (Eadwine Psalter, LXVIII, 14) and then from another younger French form cistre, later sidre, cidre "beverage made from fruits". The specific meaning "fermented beverage from apples" appears in Old French for the first time by the Norman chronicler Wace in 1130 / 1140 (Wace, conception de Nostre Dame). The Old French word *cisre (sizre) is from Gallo-Romance *cisera found in Medieval Latin by the English author Alexander Neckam (Neckam, De nominibus utensilium). It is an altered form of Church Latin sicera "fermented drink", itself borrowed from Greek sīkéra, ultimately from Hebrew šēkār, "intoxicating liquor". The cognates in the different Romance languages : Spanish, Portuguese sidra, Italian sidro, etc., in the Germanic languages : German Zider, etc. are all from French and Breton chistr, Welsh seidr (through an English form) probably too. By the 19th century, in the United States, cider referred to the expressed juice of apples, either before fermentation as sweet cider, or after fermentation, a hard cider.
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Sources: en.wikipedia.org
=== Phase 1/2 === XC-101 (XC101; XC101-D13H) – serotonin 5-HT1B and 5-HT7 receptor agonist, serotonin 5-HT1D and 5-HT1F receptor partial agonist, and serotonin 5-HT2A, 5-HT2B, and 5-HT2C receptor antagonist – migraine [29]
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Sources: en.wikipedia.org
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.
It links the peptide to serum albumin after administration, which delays removal from circulation. Reported half-life shifts from roughly half an hour to several days as a result.
Most published work tracks serum growth hormone and insulin-like growth factor 1 over time. Sampling schedules and assay methods vary enough that figures are not directly comparable across reports.
The synthetic peptide keeps the receptor-binding region of GHRH but carries substitutions that resist enzymatic cleavage. In the DAC version, an added group also anchors the molecule to albumin, extending its presence in the bloodstream.