Recombinant Human Prolyl 4-Hydroxylase Subunit beta/P4HB/PDIA1 (C-6His)

Source: E. coli. MW :55.9kD. Recombinant Human Prolyl 4-Hydroxylase Subunit Beta is produced by our E.coli expression system and the target gene encoding Asp18-Lys505 is expressed with a 6His tag at the C-terminus. Protein Disulfide-Isomerase (P4HB) is an endoplasmic reticulum lumen protein that belongs to the protein disulfide isomerase family. P4HB contains two thioredoxin domains and catalyzes the formation, breakage, and rearrangement of -S-S- bonds in proteins. P4HB is involved in hydroxylation of prolyl residues in preprocollagen. P4HB has the ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner. P4HB plays a role in both the influx and efflux of S-nitrosothiol-bound nitric oxide. 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. 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). [The UniProt Consortium]