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MA1-10032 detects PDI1P from S. cerevisiae samples.
Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, the protein seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. It may therefore cause structural modifications of exofacial proteins. Inside the cell, PDI seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, it functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). PDI may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: CaO19.12595; Eps1p; PDI; PDI1P; Protein disulfide-isomerase; Thioredoxin-related glycoprotein 1
基因别名: MFP1; PDI1; TRG1; YCL043C; YCL313; YCL43C
UniProt ID: (Baker's yeast) P17967
Entrez Gene ID: (Baker's yeast) 850314