Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

Exosome Component 9/EXOSC9 Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 51.3 kDa and the accession number is Q06265-1.