protein disulfide isomerase

E0883Hu

Sandwich

48T,96T

0.055ng/mL

0.1-40ng/mL

Serum, plasma, cell culture supernates

Human

2-8ºC

1h 30m

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. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).

57,116

5034

Cellular thyroid hormone-binding protein;CLCRP1;DSI;ERBA2L;GIT;P4Hbeta;p55;PDI;PDIA1;PHDB;PO4DB;PROHB;Prolyl 4-hydroxylase subunit beta;Protein disulfide-isomerase

P4HB

Others

PDI