Description
Description: PDIA3 Human Recombinant produced in E Coli is a single, non-glycosylated polypeptide chain containing 518 amino acids (25-505 a.a.) and having a molecular wieght of 58.5 kDa. The PDIA3 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Introduction: PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface