CJC-1295 w/ DAC

CJC-1295 with DAC is a 30-residue peptide combining the bioactive N-terminal segment of human GHRH (residues 1–29) with four substitutions that confer enzymatic resistance and a C-terminal lysine bearing the DAC linker. Albumin conjugation through DAC produces a circulating protein-peptide complex that extends plasma half-life from minutes — typical of native GHRH — into a multi-day window documented in published animal-model pharmacokinetic studies. The molecule retains affinity for the GHRH receptor on pituitary somatotrophs, engaging the same class B GPCR signaling cascade as the native ligand. Interaction profile in the literature covers cAMP activation, sustained somatotroph membrane signaling, and prolonged pulsatile growth-hormone release in feedback-control models — all reported categorically. Structural confirmation is established by mass spectrometry molecular-ion match and HPLC-validated purity on each Certificate of Analysis.

Experimental domains documented in the published literature include extended-half-life GHRH-axis investigations, albumin-conjugation pharmacokinetic studies, somatotroph-cell signaling assays under sustained agonism, and comparative work against short-acting GRF analogs to characterize the role of plasma residence in growth-hormone-axis dynamics. Investigators have also characterized the DAC construct in structure-activity studies probing how albumin binding modulates receptor engagement and downstream cAMP signaling kinetics. Use in laboratory research extends to mechanism-elucidation paradigms where the molecule serves as a tool for studying chronic versus pulsatile GHRH-receptor stimulation. The reference standard is supplied for these and equivalent in-vitro experimental contexts only, with no associated guidance for human, clinical, or veterinary application. Researchers should consult primary literature for context-specific assay conditions.

Each lot is characterized by reverse-phase HPLC for chromatographic purity and by mass spectrometry for molecular-ion confirmation against the C165H269N47O46 empirical formula. Purity is reported as an HPLC-area percentage on the Certificate of Analysis distributed with every lot, alongside the molecular-weight match within instrument tolerance. Peptide content where applicable is determined by amino-acid analysis or nitrogen-content assay following the analytical method specified on the COA. Residual solvent and water content are reported categorically when these parameters are part of the lot's release specification. The COA records the lot identifier, manufacturing date, and analytical method versions used, providing a traceable provenance chain from synthesis through release. Researchers requiring batch-level analytical detail should reference the COA distributed with the supplied material.

For laboratory storage, the lyophilized reference standard should be held at −20°C in its sealed, light-protected container until ready for analytical use. Allow vials to equilibrate to ambient temperature before opening to avoid moisture condensation on the lyophile. Reconstitution for in-vitro experimental use is typically performed in bacteriostatic water or a researcher-selected buffer compatible with the downstream assay; once reconstituted, store the working solution at 2–8°C and characterize stability in the relevant buffer prior to extended storage. Avoid repeated freeze-thaw cycles of reconstituted material — single-use aliquots are preferred for experiments where peptide integrity is assay-critical. These handling parameters reflect general best-practice for lyophilized peptide reference standards and do not constitute preparation guidance for human or veterinary application.