Protein disulfide-isomerase

E2381Mo

Sandwich

48T,96T

0.053ng/mL

0.1-40ng/mL

Serum, plasma, cell culture supernates

Mouse

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 (By similarity). 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).

57,058

18453

Cellular thyroid hormone-binding protein;Endoplasmic reticulum resident protein 59;ER protein 59;ERp;ERp59;P4HB;p55;Pd;PDI;Prolyl 4-hydroxylase subunit beta;Protein disulfide-isomerase;Thb;Thbp;

P4hb

Others

P4HB