CJC-1295 w/o DAC

CJC-1295 without DAC is a 29-residue peptide that preserves the full biologically active N-terminal segment of GHRH (residues 1–29) while incorporating substitutions at positions 2, 8, 15, and 27 that block dipeptidyl peptidase IV cleavage and other proteolytic pathways. The molecule retains GHRH-receptor affinity and engages the same class B GPCR signaling cascade as native GHRH. Pharmacokinetic descriptors documented in the literature include a short plasma half-life on the order of minutes — substantially longer than native GHRH but far shorter than the DAC-conjugated analog. Interaction profile in published work covers cAMP activation, somatotroph-cell signaling, and pulsatile growth-hormone release patterns characteristic of short-acting GRF stimulation. All activity descriptors here are framed as documented in published work rather than as effects of the supplied product. Structural confirmation is established by mass spectrometry and HPLC-validated purity on each Certificate of Analysis.

Experimental domains documented in the published literature include short-acting GHRH-axis investigations, pulsatile-versus-sustained agonism comparative studies, somatotroph-cell signaling assays under transient receptor engagement, and structure-activity work probing the role of individual amino-acid substitutions in conferring proteolytic resistance. Investigators have also used the molecule as a control alongside the DAC-conjugated variant to dissect plasma-residence effects from intrinsic receptor-engagement properties. Use in laboratory research extends to feedback-loop modeling where transient GHRH-receptor activation is the experimental variable. 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 protocols and validated assay controls.

Each lot is characterized by reverse-phase HPLC for chromatographic purity and by mass spectrometry for molecular-ion confirmation. 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 rather than rely on category-level summaries.

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.