P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.
P4HB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 512 amino acids (18-508 a.a.) and having a molecular mass of 57.5 kDa. The P4HB is fused to a 21 amino acid His Tag and purified by conventional chromatography.
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