Type III iodothyronine deiodinase (Dio3) Recombinant Protein | Dio3 recombinant protein

Recombinant Rat Type III iodothyronine deiodinase (Dio3), partial

Cat. Num. AAA1116133

• Gene Names: Dio3; 5DIII; DIOIII
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Type III iodothyronine deiodinase (Dio3); Recombinant Rat Type III iodothyronine deiodinase (Dio3); partial; 5DIII; DIOIII; Type 3 DI; Type-III 5'-deiodinase; Dio3 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: 63-304aa (170:U->missing); partial
• Sequence: DFLCIRKHFLRRRHPDHPEPEVELNSEGEEMPPDDPPICVSDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVRPDGFQSQRILDYAQGTRPLVLNFGSCTPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDGWVTTDSPYVIPQHRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQSGTIMYQGGRGPDGYQVSELRTWLERYDEQLHGTRPRRL

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

SDS-PAGE

Test Data

(MBS1116133 Recombinant Rat Thyroxine 5-deiodinase(Dio3), Expression Region: 63-304aa is missing the aa ‘U’ at the 170 site (see dash -, line Sbjct 121-179).)

Related Product Information for Dio3 recombinant protein

Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing prature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development.

References

Genome sequence of the Brown Norway rat yields insights into mammalian evolution.Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.Nature 428:493-521(2004) Cloning and expression of a cDNA for a mammalian type III iodothyronine deiodinase.Croteau W., Whittemore S.L., Schneider M.J., St Germain D.L.J. Biol. Chem. 270:16569-16575(1995)

NCBI and Uniprot Product Information

• NCBI GI #: 255982585
• NCBI GeneID: 29475
• NCBI Accession #: NP_058906.3
• NCBI GenBank Nucleotide #: NM_017210.3
• UniProt Accession #: P49897
• Molecular Weight: 29.5 kDa
• NCBI Official Full Name: thyroxine 5-deiodinase
• NCBI Official Synonym Full Names: deiodinase, iodothyronine, type III
• NCBI Official Symbol: Dio3
• NCBI Official Synonym Symbols: 5DIII; DIOIII
• NCBI Protein Information: thyroxine 5-deiodinase
• UniProt Protein Name: Thyroxine 5-deiodinase
• Protein Family: Thyroxine 5-deiodinase
• UniProt Gene Name: Dio3
• UniProt Synonym Gene Names: Itdi3; Txdi3
• UniProt Entry Name: IOD3_RAT

NCBI Description

The protein encoded by this intronless gene belongs to the iodothyronine deiodinase family. It catalyzes the inactivation of thyroid hormone by inner ring deiodination of the prohormone thyroxine (T4) and the bioactive hormone 3,3',5-triiodothyronine (T3) to inactive metabolites, 3,3',5'-triiodothyronine (RT3) and 3,3'-diiodothyronine (T2), respectively. This enzyme is highly expressed in the pregnant uterus, placenta, fetal and neonatal tissues, suggesting that it plays an essential role in the regulation of thyroid hormone inactivation during embryological development. It contains a selenocysteine (Sec) residue, which is essential for efficient enzyme activity. The selenocysteine is encoded by the UGA codon, which normally signals translation termination. The 3' UTR of Sec-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. [provided by RefSeq, Jul 2008]

Uniprot Description

DIO3: Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development. Belongs to the iodothyronine deiodinase family.

Protein type: EC 1.97.1.11; Oxidoreductase; Membrane protein, integral

Cellular Component: endosome membrane; integral to membrane; plasma membrane

Molecular Function: thyroxine 5'-deiodinase activity; thyroxine 5-deiodinase activity

Biological Process: hormone biosynthetic process; positive regulation of multicellular organism growth; response to hypoxia; thyroid hormone catabolic process; thyroid hormone metabolic process