Modified GRF (1-29) is a synthetic peptide corresponding to the N-terminal 29–amino acid region of growth hormone–releasing factor (GRF), incorporating targeted amino acid substitutions to increase biochemical stability in experimental systems. This truncated analogue represents the GRF domain commonly used in laboratory studies focused on endocrine signaling and peptide–receptor interaction workflows.

The compound is commonly referenced in the scientific literature as CJC-1295 without DAC, distinguishing it from affinity-modified, extended-duration variants. In research settings, this non-DAC format is used to investigate receptor engagement, early signal initiation, and temporal pathway dynamics under controlled preclinical conditions.

This material is supplied strictly for research use in in-vitro experiments and in-vivo animal model studies.

Sequence: Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Leu-Ser-Arg-NH₂

Molecular Formula: C₁₅₂H₂₅₂N₄₄O₄₂
Molar Mass: 3368.7 g/mol
Synonyms: Mod GRF 1-29, CJC-1295 (no DAC)

The substitution of D-alanine at position 2 is used in experimental peptide design to reduce susceptibility to enzymatic cleavage observed for native sequence motifs in biological matrices. C-terminal amidation is included to support conformational stability and consistent receptor-interaction behavior during in-vitro analysis.

Modified GRF (1-29) is used in laboratory research to investigate growth hormone–releasing hormone receptor (GHRHR) activation and associated intracellular signaling cascades. The peptide is applied as a tool compound for studying ligand–receptor dynamics, receptor kinetics, and second-messenger pathway modulation in controlled experimental systems.

Common experimental applications include:

• GHRHR binding affinity and kinetics assays
• Adenylate cyclase activation and cyclic AMP signaling studies
• Structure–activity relationship (SAR) comparisons among GRF(1-29) analogues
• Endocrine and neuroendocrine signaling investigations in cellular and animal research models

The absence of DAC modification is leveraged in experimental design to evaluate transient signaling events without long-acting affinity contributions.

Modified GRF (1-29) interacts with the growth hormone–releasing hormone receptor (GHRHR), a class B G protein–coupled receptor frequently studied for its primary coupling to G_s signaling. In canonical models, receptor activation stimulates adenylate cyclase activity, increasing intracellular cyclic AMP and engaging PKA-linked phosphorylation events and downstream transcriptional regulators.

This signaling axis is used in preclinical research to characterize receptor specificity, signal amplification, temporal activation patterns, and feedback regulation mechanisms within endocrine and neuroendocrine model systems.

Preclinical studies employing Modified GRF (1-29) have focused on receptor activation profiles, comparative potency among GRF analogues, and intracellular signaling kinetics in cell-based systems. In vivo animal studies have been used to examine endocrine-axis signaling regulation and peptide distribution characteristics using established laboratory endpoints.

These investigations contribute to foundational knowledge regarding peptide hormone signaling mechanisms and receptor pharmacology. All reported findings are derived exclusively from non-clinical experimental systems.

This peptide is supplied as a lyophilized solid intended to support stability during storage and transport prior to laboratory handling. Product identity and purity are verified using established analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry (MS).

All materials are manufactured under controlled laboratory conditions to support batch-to-batch consistency for research reproducibility.

1. L. Jetté et al., “Human Growth Hormone-Releasing Factor (hGRF)1–29-Albumin Bioconjugates Activate the GRF Receptor on the Anterior Pituitary in Rats: Identification of CJC-1295 as a Long-Lasting GRF Analog,” Endocrinology, vol. 146, no. 7, pp. 3052–3058, 2005. [PubMed]
2. L. A. Frohman et al., “Rapid enzymatic degradation of growth hormone-releasing hormone by plasma in vitro and in vivo to a biologically inactive product cleaved at the NH₂ terminus,” J. Clin. Invest., vol. 78, no. 4, pp. 906–913, 1986. [PubMed] [PMC]
3. J. Izdebski et al., “New potent hGH-RH analogues with increased resistance to enzymatic degradation,” J. Pept. Sci., vol. 8, no. 7, pp. 289–296, 2002. [PubMed]

ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATONAL AND EDUCATIONAL PURPOSES ONLY.

The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.

For Laboratory Research Only. Not for human use, medical use, diagnostic use, or veterinary use.