Recombinant Human Protein Disulfide-Isomerase A6/PDIA6 (C-6His)
|Alternative Name :||Protein Disulfide-Isomerase A6, Endoplasmic Reticulum Protein 5, ER Protein 5, ERp5, Protein Disulfide Isomerase P5, Thioredoxin Domain-Containing Protein 7, PDIA6, ERP5, P5, TXNDC7|
|Amount :||50 µg|
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.
|Content :||Supplied as a 0.2 µm filtered solution of 20mM TrisHCl, 150mM NaCl, 10% Glycerol, pH 8.0.|
|Amino acid sequence :||Recombinant Human Protein Disulfide-Isomerase A6 is produced by our Mammalian expression system and the target gene encoding Leu20-Leu440 is expressed with a 6His tag at the C-terminus.|