Abcam, ab95910, Recombinant E. coli Thioredoxin reductase protein

Size: 100µg / 500µg
Recombinant E. coli Thioredoxin reductase protein is a Escherichia coli K-12 Full Length protein, in the 1 to 321 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec, FuncS.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:SDS-PAGE, FuncS, Mass SpecSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity is 4-5 units/ml, and was measured in a coupled assay with DTNB and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.,
Accession:P0A9P4,
Animal free:No,
Carrier free:No,
Species:Escherichia coli K-12,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Thioredoxin reductase also known as TrxR or TXNRD is an enzyme that reduces thioredoxin and other substrates. It is a selenoprotein with a molecular mass of approximately 55 kDa and contains a significant selenocysteine residue at its active site. Thioredoxin reductase exists in cytosol mitochondria and sometimes in the endoplasmic reticulum across various cell types allowing it to fulfill its role in maintaining cellular redox homeostasis by facilitating the reduction of thioredoxin.
Biological function summary
Thioredoxin reductase participates in several critical cellular processes beyond just reducing substrates. It acts as an important player in antioxidant defense cellular signaling and apoptosis. As part of the thioredoxin system which often works closely with other antioxidant systems it plays a role in detoxifying harmful reactive oxygen species. It is not typically part of larger protein complexes but interacts functionally with many proteins to regulate redox signaling pathways.
Pathways
Thioredoxin reductase engages in the regulation of redox signaling and is active in the thioredoxin system pathway. This pathway plays an important role in controlling enzymatic processes that guard cells against oxidative stress. Thioredoxin reductase is also involved in the NADPH-dependent thioredoxin system alongside thioredoxin and NADPH. The enzyme is correlated with the activity of glutathione peroxidase emphasizing its role in redox balance within the cell.
Thioredoxin reductase is implicated in the progression of cancer and cardiovascular diseases. Its overexpression is often observed in cancerous cells where it aids in cell survival and proliferation by managing oxidative stress levels. In cardiovascular diseases altered thioredoxin reductase activity relates to endothelial dysfunction. The enzyme interacts with proteins like thioredoxin to impact disease mechanisms highlighting its importance in therapeutic targets for these conditions.