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Protein disulfide isomerase, also known as proline 4-hydroxylase β subunit (P4HB), cellular thyroid hormone binding protein (p55) and glutathione-insulin transhydrogenase, is a kind of peripheral membrane protein belonging to the protein disulfide isomerase family. It contains two thioredoxin domains that catalyze the formation, breaking, and rearrangement of disulfide bonds. P4HB was located near the CD4 rich area on the surface of lymphocytes. In melansome components, P4HB reduces and activates the fusion properties of HIV-1 gp120 surface proteins, thereby allowing HIV-1 to enter the cell. P4HB acts as a chaperone, inhibiting the aggregation of misfolded proteins. P4HB may be involved with other molecular chaperones in the structural modification of TG precursors in hormone biosynthesis.