Anti-PDI

Anti-PDI Antibody was prepared from monospecific antiserum by delipidation and defibrination. A BLAST analysis was used to suggest cross-reactivity with PDI from Human, Mouse, Rat, Dog, Hamster, Monkey, Guinea pig, Bovine, Sheep, Pig, and Xenopus based on 100% homology with the immunizing sequence. Cross-reactivity with PDI from other sources has not been determined. Chaperones, Organelle Markers research. Protein function: 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. [The UniProt Consortium]