Thioredoxin reductase 1, cytoplasmic is a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine (Sec) residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenocysteine-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms.

Rat Thioredoxin reductase (TRXR) ELISA Kit employs a two-site sandwich ELISA to quantitate TXNRD1 in samples. An antibody specific for TXNRD1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyTXNRD1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for TXNRD1 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of TXNRD1 bound in the initial step. The color development is stopped and the intensity of the color is measured.

Rat Thioredoxin reductase (TRXR) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.

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