功能： catalytic activity:2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.,function:Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.,miscellaneous:Irreversibly inactivated by overoxidation of Cys-124 (to Cys-SO(3)H) upon oxidative stress.,miscellaneous:The active site is the redox-active Cys-124 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.,similarity:Belongs to the ahpC/TSA family.,similarity:Contains 1 thioredoxin domain.,subunit:Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.,
相關產(chǎn)品： RS0001,RS0002,YM3028,YM3029
細胞定位： Cytoplasm . Endoplasmic reticulum . Cotranslationally translocated to and retained within the endoplasmic reticulum. A small fraction of the protein is cytoplasmic. .
功能： catalytic activity:2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.,function:Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.,miscellaneous:Irreversibly inactivated by overoxidation of Cys-124 (to Cys-SO(3)H) upon oxidative stress.,miscellaneous:The active site is the redox-active Cys-124 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.,similarity:Belongs to the ahpC/TSA family.,similarity:Contains 1 thioredoxin domain.,subunit:Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.,
相關產(chǎn)品： RS0001,RS0002,YM3028,YM3029
細胞定位： Cytoplasm . Endoplasmic reticulum . Cotranslationally translocated to and retained within the endoplasmic reticulum. A small fraction of the protein is cytoplasmic. .
科研貨號： PLA020423
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