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These structural characteristics hold significant value for the design of novel inhibitors

Product Specifications Compound: CJC-1295 with DAC Class: Synthetic GHRH analog with albumin-binding modification Origin: Modified GHRH (1-29) analog with N-terminal Drug Affinity Complex Molecular Weight: ~3647 Da Form: Lyophilized powder Vial Size: 5mg in 3mL glass vial Purity: 99%+ verified by HPLC and mass spectrometry (See COAs) Research Background CJC-1295 with DAC has been investigated in research literature across several scientific contexts: GHRH receptor pharmacology investigations into receptor binding kinetics, signal transduction, and cellular response mechanisms in pituitary cell models Albumin-binding peptide research studies examining how covalent serum albumin binding via maleimidopropionic acid modification affects peptide half-life, distribution, and stability properties Peptide half-life engineering analytical chemistry research on extended-duration peptide analogs and the structural modifications that enable prolonged biological activity Comparative GHRH analog research studies positioning CJC-1295 with DAC alongside other modified GHRH peptides (including Sermorelin and Tesamorelin) in cellular research contexts Structure-activity relationships peptide chemistry research on how DAC modification affects receptor binding affinity compared to non-modified GHRH analogs Cellular signaling pathway research investigations into GHRH receptor activation and downstream cellular signaling cascades CJC-1295 with DAC was originally developed by ConjuChem Biotechnologies as part of their broader Drug Affinity Complex peptide research platform, which utilized albumin-binding chemistry to extend peptide half-life across multiple research compound development programs