BPC-157 & TB-500 Blend 20mg

This is a two-component lyophilized preparation supplied in a single vial and resolved by component on the certificate of analysis. BPC-157 is a synthetic pentadecapeptide of sequence Gly-Glu-Pro-Pro- Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, proline-rich and free of cysteine. TB-500 is the full-length 43-residue thymosin beta-4 sequence and carries the seven-residue LKKTETQ actin-binding motif; the two peptides are chemically unrelated and are characterised independently.

For the TB-500 component, the characterised molecular partner is monomeric G-actin, bound through the LKKTETQ motif; complex formation is quantified in vitro by pyrene-actin polymerisation assays, DNase I inhibition assays and isothermal titration calorimetry, with reported dissociation constants in the low-micromolar range in defined buffer systems. For the BPC-157 component, no high-affinity receptor has been established in the peer-reviewed literature and no dissociation constant against a defined binding site has been reported; in-vitro work is described instead as immunoblot and enzymatic readouts in cultured cell lines and lysates.

Primary literature covering the actin-binding chemistry of the thymosin beta-4 sequence and the synthesis and analytical characterisation of the pentadecapeptide GEPPPGKPADDAGLV is indexed in PubMed and in peptide and cytoskeletal biochemistry journals. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.