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| Product Name | Protein Disulfide-isomerase, active (P4HB), Recombinant, Human |
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| Description | Purity ≥95% as determined by SDS-PAGE and HPLC. This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. (ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997). Biological Activity: Thiol Protein Reductase Activity is 0.001 Δ650nm/ min-2, determined by measuring the turbidity increase at 650 nm due to insulin reduction.The |
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| Size | 20ug, 100ug, 250ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | PDI, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 |
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| Gene, Accession, CAS # | PDIA1_HUMAN, SwissProt: P07237 |
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| Catalog # | 348217 |
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| Order / More Info | Protein Disulfide-isomerase, active (P4HB), Recombinant, Human from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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