TB-500 10mg

TB-500 is a synthetic peptide corresponding to the thymosin beta-4 sequence, a member of the beta- thymosin family of small, highly acidic, intrinsically disordered polypeptides. Its defining structural element is the central seven-residue actin-binding motif LKKTETQ, flanked by an N-terminal helical segment and a C-terminal region that both fold upon binding. The peptide contains no cysteine residues and therefore no disulfide bridge.

The characterised molecular partner is monomeric G-actin, engaged through the LKKTETQ motif and the flanking helices. Complex formation is quantified in vitro by pyrene-actin polymerisation assays, DNase I inhibition assays, fluorescence anisotropy and isothermal titration calorimetry, with reported dissociation constants in the low-micromolar range under defined ionic-strength and buffer conditions. Structural characterisation of the peptide-actin interface is reported from X-ray crystallography and NMR of defined complexes.

Primary literature on beta-thymosin chemistry, the LKKTETQ actin-binding motif and structural characterisation of peptide-actin complexes is indexed in PubMed and in cytoskeletal biochemistry and structural biology journals. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.