If you have been reading about Mod GRF(1-29) 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 2026-08-01. Numbers and descriptions here follow the published literature rather than marketing material.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular weight, DAC form | About 3647 Da | Varies with salt form |
| Molecular weight, non-DAC form | About 3358 Da | MOD GRF(1-29) |
| Solubility class | Water soluble | Also dissolves in polar solvents |
| Reported half-life, DAC form | About five to eight days | Values from human studies |
| Common synonyms | CJC-1295; MOD GRF(1-29) | Name depends on variant |
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.
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.
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.
== Invertebrates == In some invertebrates, such as Porifera, Cnidaria, Ctenophora, and some triploblasts (namely the acoelomates), the term "mesenchyme" refers to a more-or-less solid but loosely organized tissue that consists of a gel matrix (the mesoglea) with various cellular and fibrous inclusions, located between the epidermis and the gastrodermis (non-triploblast animals usually are considered to lack "connective" tissue). In some cases, the mesoglea is noncellular.
=== Hormonal and dietary === Insulin is by far the most important of the hormones that have direct or indirect effects on glucokinase expression and activity in the liver. Insulin appears to affect both glucokinase transcription and activity through multiple direct and indirect pathways. While rising portal vein glucose levels increase glucokinase activity, the concomitant rise of insulin amplifies this effect by induction of glucokinase synthesis. Glucokinase transcription begins to rise within an hour of rising insulin levels. Glucokinase transcription becomes nearly undetectable in prolonged starvation, severe carbohydrate deprivation, or untreated insulin-deficient diabetes. The mechanisms by which insulin induces glucokinase may involve both of the major intracellular pathways of insulin action, the extracellular signal-regulated kinase (ERK 1/2) cascade, and the phosphoinositide 3-kinase (PI3-K) cascade. The latter may operate via the FOXO1 transactivator. However, as would be expected given its antagonistic effect on glycogen synthesis, glucagon and its intracellular second messenger cAMP suppresses glucokinase transcription and activity, even in the presence of insulin. Other hormones such as triiodothyronine (T3) and glucocorticoids provide permissive or stimulatory effects on glucokinase in certain circumstances. Biotin and retinoic acid increase GCK mRNA transcription as well as GK activity. Fatty acids in significant amounts amplify GK activity in the liver, while long chain acyl CoA inhibits it.
Sjögren's disease may be excluded in people with past head and neck radiation therapy, active hepatitis C confirmed with a positive PCR test, acquired immunodeficiency syndrome, sarcoidosis, amyloidosis, graft-versus-host disease, and IgG4-related disease. Patients using anticholinergic drugs must stop using them for some time before being evaluated for symptoms of dryness.
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Sources: en.wikipedia.org
=== OXGR1 receptor-dependent bioactions === OXGR1 (also known as GPR99) is a G protein-coupled receptor, i.e., a receptor located on the surface membrane of cells that binds certain ligands and is thereby stimulated to activate G proteins that elicit pre-programmed responses in their parent cells. OXGR1 was identified as a receptor for: a) α-ketoglutarate in 2004; b) three leukotrienes viz., leukotrienes E4, C4, and D4 in 2013. and c) itaconate in 2023. These ligands have the following relative potencies in stimulating responses in OXGR1-bearing cells (Note that LTE4 can stimulate OXGR1 at concentrations far lower than those of the other four ligands):
This is because the fundamental principle of labour law is that employees' unequal bargaining power justifies substitution of rules in property and contract with positive social rights so that people may earn a living to fully participate in a democratic society. The EU's competences generally follow principles codified in the Community Charter of the Fundamental Social Rights of Workers 1989, introduced in the "social chapter" of the Treaty of Maastricht. Initially the UK had opted-out, because of opposition by the Conservative Party, but was acceded to when the Labour Party won the 1997 general election in the Treaty of Amsterdam.
Theca cells are responsible for synthesizing androgens, providing signal transduction between granulosa cells and oocytes during development by the establishment of a vascular system, providing nutrients, and providing structure and support to the follicle as it matures. Theca cells are responsible for the production of androstenedione, which is supplied to the neighboring granulosa cells where it is converted into estrone (a weak estrogen) by the enzyme aromatase, and then further converted into estradiol (a strong estrogen) by the enzyme 17β-HSD1. FSH stimulates granulosa cells to synthesize aromatase and 17β-HSD, which is necessary for this process.
Serum albumins are the most common plasma proteins, and they are responsible for maintaining the osmotic pressure of the blood. Without albumins, the consistency of blood would be closer to that of water. The increased viscosity of blood prevents fluid from entering the bloodstream from outside the capillaries. Albumins are produced in the liver, assuming the absence of a hepatocellular deficiency.
Sources: en.wikipedia.org
It is a synthetic peptide modeled on growth hormone-releasing hormone. The molecule is used in research on pituitary growth hormone secretion. It differs from the natural hormone through several stabilizing substitutions.
The DAC form carries a maleimide group that binds albumin and extends circulation time. The non-DAC form lacks this group and clears much faster. Both share the same receptor-binding core.
It targets the growth hormone-releasing hormone receptor on pituitary somatotroph cells. Activation raises cyclic AMP and promotes growth hormone release. Normal feedback pathways remain part of the response.
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.