| Description: | P4HB protein, a multifunctional entity, catalyzes disulfide bond processes at the cell surface and intracellularly. Serving as a reductase, it modifies exofacial proteins and participates in nascent protein disulfide bond formation. Regulated by FAM20C phosphorylation, P4HB acts as a chaperone at elevated concentrations, preventing misfolded protein aggregation, and exhibits anti-chaperone activity at lower concentrations, promoting aggregation. As a structural subunit in enzymes like prolyl 4-hydroxylase and MTTP, and as a receptor for LGALS9, P4HB plays diverse roles in cellular processes, emphasizing its importance in protein folding, redox regulation, and cell migration. P4HB Protein, Human (HEK293, His) is the recombinant human-derived P4HB protein, expressed by HEK293, with C-6*His labeled tag. The total length of P4HB Protein, Human (HEK293, His) is 488 a.a., with molecular weight of ~58.9 kDa. |
