P4HB polyclonal antibody

Oxidoreductase-protein disulfide isomerase (PDI) is a homodimer consisting of subunits that catalyzes thiol-disulfide exchange, mediates folding of newly synthesized proteins and functions as a molecular chaperone. PDI localizes to the lumen of the endoplasmic reticulum (ER), where in conjunction with folding-helper proteins, such as immunoglobulin heavy chain binding protein (BiP), mediates tertiary and quaternary protein-processing. Cell surface PDI induces sulfhydryl-mediated conformational changes in integrin-mediated adhesion receptor-ligand interactions, thereby regulating integrin responses and cell adhesion. Additionally, PDI functions as a subunit of two more complex enzyme systems: the prolyl-4-hydroxylase and the triacylglycerol transfer proteins.

Cellular thyroid hormone binding protein; Cellular thyroid hormone-binding protein; Collagen prolyl 4 hydroxylase beta; Disulphide Isomerase; DSI; EC 5.3.4.1; Endoplasmic reticulum resident protein 59; ER protein 59; ERBA2L; ERp59; GIT; Gltathione insulin transhydrogenase; Glutathione insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PDIA1; PDIR; PHDB; PO4DB; PO4HB; Procollagen proline 2 oxoglutarate 4 dioxygenase (proline 4 hydroxylase) beta polypeptide (pro

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .