Search Thermo Fisher Scientific
Search Thermo Fisher Scientific
Invitrogen
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: CaO19.12595; Eps1p; PDI; PDI1P; Protein disulfide-isomerase; Thioredoxin-related glycoprotein 1
Gene Aliases: MFP1; PDI1; TRG1; YCL043C; YCL313; YCL43C
UniProt ID: (Baker's yeast) P17967
Entrez Gene ID: (Baker's yeast) 850314
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