PDIA6 Human, Active
Source: Escherichia Coli.Sterile Filtered colorless solution.PDIA6 belongs to the protein disulfide isomerase family (PDI) . PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDIA6 functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6, also has a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.PDIA6 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 442 amino acids (20-440 a.a.) and having a molecular mass of 48.5kDa. The PDIA6 is purified by proprietary chromatographic techniques.
Product Specifications
Product Name Alternative
Applications
Functional Assay
Purification
Greater than 90.0% as determined by SDS-PAGE.
Components
The PDIA6 solution (1 mg/mL) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 50mM NaCl.
Storage Conditions
Applications Notes
Specific activity > 20 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of INS in the presence of DTT.
Amino Acids
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