Recombinant Human Protein disulfide-isomerase (P4HB)
Description
Purity > 90% as determined by SDS-PAGE. MW: 59.3kDa. Full Length of Mature Protein: 18-508aa. N-terminal 6xHis-tagged. Homo sapiens (Human). This multifunctional protein catalyzes the formation, breakage and rearrangent of disulfide bonds. At the cell surface, ses 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, ses 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.