|Calculated MW||55.7 kDa|
|Other Names||Thioredoxin Reductase, GRIM-12, MGC9145, TR, TR1, TRXR1, TXNR.|
|Sequence||MGSSHHHHHH SSGLVPRGSH MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQA LQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLG IPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQI EAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQA GRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGC|
|Storage||-80°C; 0.5 mg/ml solution in PBS (pH 7.4) containing 10% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Thioredoxin reductase 1, cytoplasmic is an enzyme that in humans is encoded by the TXNRD1 gene. This gene encodes 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. Inhibition of TXNRD1 activity may provide for potential treatments of cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases
Gasdaska P.Y.,et al.FEBS Lett. 373:5-9(1995).
Koishi R.,et al.J. Biol. Chem. 272:2570-2577(1997).
Hofman E.R.,et al.Mol. Cell. Biol. 18:6493-6504(1998).
Rundloef A.-K.,et al.Free Radic. Biol. Med. 36:641-656(2004).
Schuetze N.,et al.Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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