| Description: | Trigger factor protein, crucial to protein export, functions as a chaperone and peptidyl-prolyl cis-trans isomerase. In its chaperone role, it maintains nascent polypeptides in an open conformation, aiding proper protein folding. Simultaneously, its isomerase activity refines the conformational landscape by isomerizing prolyl peptide bonds. Trigger factor's multifaceted involvement underscores its significance in orchestrating cellular protein homeostasis and export mechanisms. Trigger factor Protein, E.coli (P.pastoris, His) is the recombinant E. coli-derived Trigger factor protein, expressed by P. pastoris, with N-His labeled tag. The total length of Trigger factor Protein, E.coli (P.pastoris, His) is 432 a.a., with molecular weight (affected by relative charge) of ~60 KDa. |
