Recombinant Human Protein disulfide-isomerase protein (P4HB) (Active)
Description
Purity > 95% as determined by SDS-PAGE and HPLC. MW: 56.6kDa. Partial: 19-456aa. N-terminal 6xHis-tagged. Homo sapiens (Human). This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997}.