Thioredoxin reductase 2 Recombinant Protein | Q9NNW7 recombinant protein

Recombinant Human Thioredoxin reductase 2, mitochondrial

Cat. Num. AAA1354229

• Gene Names: TXNRD2; TR; TR3; SELZ; TRXR2; TR-BETA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Thioredoxin reductase 2; Recombinant Human Thioredoxin reductase 2; mitochondrial; Selenoprotein Z; SelZTR-beta; Thioredoxin reductase TR3; Q9NNW7 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 37-524aa; Full Length
• Sequence: QRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG
• Sequence Length: 338

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for Q9NNW7 recombinant protein

Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.

References

Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases.Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.J. Biol. Chem. 274:24522-24530(1999) Cloning, sequencing and functional expression of a novel human thioredoxin reductase.Gasdaska P.Y., Berggren M.M., Berry M.J., Powis G.FEBS Lett. 442:105-111(1999) Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization.Miranda-Vizuete A., Damdimopoulos A.E., Pedrajas J.R., Gustafsson J.-A., Spyrou G.Eur. J. Biochem. 261:405-412(1999) Toji S., Yano M., Tamai K.Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif.Lescure A., Gautheret D., Carbon P., Krol A.J. Biol. Chem. 274:38147-38154(1999) Kim J.-R., Lee Y.H., Lee S.-R., Kim B.H., Rhee S.G., Kim J.H.The DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999) Heterogeneity within animal thioredoxin reductases evidence for alternative first exon splicing.Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.J. Biol. Chem. 276:3106-3114(2001) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)

NCBI and Uniprot Product Information

• NCBI GI #: 542029077
• NCBI GeneID: 10587
• NCBI Accession #: NP_001269441.1
• NCBI GenBank Nucleotide #: NM_001282512.1
• UniProt Accession #: Q9NNW7; O95840; Q96IJ2; Q9H2Z5; Q9NZV3; Q9NZV4; Q9P2Y0; Q9P2Y1; Q9UQU8
• Molecular Weight: 68.9 kDa
• NCBI Official Full Name: thioredoxin reductase 2, mitochondrial isoform 2
• NCBI Official Synonym Full Names: thioredoxin reductase 2
• NCBI Official Symbol: TXNRD2
• NCBI Official Synonym Symbols: TR; TR3; SELZ; TRXR2; TR-BETA
• NCBI Protein Information: thioredoxin reductase 2, mitochondrial
• UniProt Protein Name: Thioredoxin reductase 2, mitochondrial
• Protein Family: Thioredoxin reductase
• UniProt Gene Name: TXNRD2
• UniProt Synonym Gene Names: KIAA1652; TRXR2; SelZ
• UniProt Entry Name: TRXR2_HUMAN

NCBI Description

This gene encodes a member of the class I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein is a selenocysteine-containing flavoenzyme that maintains thioredoxins in a reduced state, thereby playing a key role in regulating the cellular redox environment. Mammals have three related thioredoxin reductases. This gene encodes a mitochondrial form important for scavenging of reactive oxygen species in mitochondria. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Sep 2013]

Uniprot Description

TXNRD2: Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 1.8.1.9; Nuclear receptor co-regulator; Nucleotide Metabolism - pyrimidine; Oxidoreductase

Chromosomal Location of Human Ortholog: 22q11.21

Cellular Component: mitochondrial matrix; mitochondrion

Molecular Function: FAD binding; protein binding; thioredoxin-disulfide reductase activity

Biological Process: cell redox homeostasis; response to oxygen radical; response to reactive oxygen species