CJC-1295 with DAC

About This Research Material

This listing supplies CJC-1295 with DAC (2 mg) as a lyophilized reference peptide for in-vitro and preclinical laboratory work. CJC-1295 is a synthetic analog of the first 29 residues of growth-hormone-releasing hormone — the GRF(1-29) fragment — carrying a small set of amino-acid substitutions that improve resistance to enzymatic cleavage. The defining structural feature of this version is the DAC group: a Drug Affinity Complex built from a maleimidopropionyl lysine linker. That reactive tether is designed to form a covalent bond with a free cysteine thiol on circulating serum albumin, so in a research setting the peptide is studied as an albumin-binding, long-acting GRF analog rather than as a short-lived free peptide. The molecular formula for this product is C165H269N47O46, and it is registered under CAS 863288-34-0.

The distinction between the DAC and non-DAC forms matters when planning bench work. Without the DAC linker, modified GRF(1-29) (sometimes catalogued as CJC-1295 'no-DAC' or Mod-GRF 1-29) behaves as a comparatively short-lived analog; the DAC modification is what confers the extended albumin-association profile that researchers characterize in this material. All descriptions below concern the research substance itself — its documented study history and its analytical fingerprint — and make no claim about outcomes in humans or animals.

What Has Been Studied in Preclinical Models

Published investigations of CJC-1295 with DAC are laboratory and preclinical in nature. As a GHRH-receptor-directed analog, it has been used in cell-based receptor-binding and signaling assays that probe the class B G-protein-coupled GHRH receptor and downstream cAMP responses in cultured pituitary-derived cells. The albumin-affinity behavior conferred by the maleimide-DAC chemistry has itself been a subject of characterization work, since the thiol-maleimide conjugation is the mechanistic basis for the compound's extended plasma-association profile observed in animal models.

• In-vitro GHRH-receptor binding and cAMP-signaling assays in pituitary-derived cell lines.
• Characterization of maleimide-thiol conjugation to serum albumin as a plasma-association (half-life-extension) strategy.
• Rodent-model pharmacokinetic studies comparing DAC and non-DAC GRF analog clearance.
• Stability and receptor-selectivity assays used to fingerprint peptide behavior under controlled conditions.

Analytical Characterization

Each research lot is supplied as a lyophilized powder and characterized before release so the material matches the sequence and mass expected for the DAC-modified GRF(1-29) analog. Identity and purity are established with orthogonal methods, keeping the two questions separate: purity asks how much of the sample is the target peptide, while identity confirms the target is the correct molecule with the maleimide-lysine linker intact.

• RP-HPLC purity: quantified by peak-area integration and reported on the COA (≥98% for this product). The chromatogram resolves the main peak from truncated sequences and process-related impurities.
• Mass-spectrometry identity: ESI-MS or MALDI-TOF confirms the observed mass against the theoretical value for C165H269N47O46, verifying the intact DAC-conjugated sequence.
• Supporting data: appearance, net peptide content, and residual-solvent or water-content checks where applicable.

The Certificate of Analysis (COA) accompanying each product is the definitive analytical record for that specific lot. Because purity and mass can vary slightly between synthesis batches, researchers should reference the COA tied to the lot number received rather than generic specifications when documenting experimental inputs. Because the maleimide moiety in the DAC linker is thiol-reactive, standard laboratory handling calls for reconstitution with a thiol-free research-grade solvent, keeping the sealed vial equilibrated to room temperature before opening to limit condensation on the hygroscopic solid, and aliquoting the stock to minimize freeze-thaw cycles. Detailed temperature and stability windows appear in the storage table on this page.