Isocitrate dehydrogenase [NAD] subunit beta Recombinant Protein | IDH3B recombinant protein

Recombinant Human Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial

Cat. Num. AAA1204109

• Gene Names: IDH3B; RP46; H-IDHB
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Isocitrate dehydrogenase [NAD] subunit beta; Recombinant Human Isocitrate dehydrogenase [NAD] subunit beta; mitochondrial; Isocitric dehydrogenase subunit beta; NAD(+)-specific ICDH subunit beta; IDH3B 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: 35-385aa; Full Length
• Sequence: ASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS
• Sequence Length: 385

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

SDS-PAGE

Product Categories/Family for IDH3B recombinant protein

Metabolism

References

Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase beta subunit isoform.Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S., Lee I.J., Song B.J., Huh T.-L.J. Biol. Chem. 274:36866-36875(1999) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and comparative analysis of human chromosome 20.Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.Nature 414:865-871(2001)

NCBI and Uniprot Product Information

• NCBI GI #: 28178821
• NCBI GeneID: 3420
• NCBI Accession #: NP_008830.2
• NCBI GenBank Nucleotide #: NM_006899.3
• UniProt Accession #: O43837; O95106; Q5JXS8; Q9NQ06; Q9NQ07; Q9NUZ0; Q9UEX0; Q9UG99; B2RDR1; D3DVX2; D3DVX3
• Molecular Weight: 65.8 kDa
• NCBI Official Full Name: isocitrate dehydrogenase
• NCBI Official Synonym Full Names: isocitrate dehydrogenase 3 (NAD+) beta
• NCBI Official Symbol: IDH3B
• NCBI Official Synonym Symbols: RP46; H-IDHB
• NCBI Protein Information: isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
• UniProt Protein Name: Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
• Protein Family: Isocitrate dehydrogenase
• UniProt Gene Name: IDH3B
• UniProt Entry Name: IDH3B_HUMAN

NCBI Description

Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the beta subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

IDH3B: a enzyme that that catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate (alpha-KG), requiring nicotinamide adenine dinucleotide (NAD) as a cofactor. The holoenzyme is a heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1. IDH3 is a mitochondrial enzyme that functions in the Krebs cycle, which generates substrates for cellular respiration. Alpha-KG can exit the mitochondria and enter other cellular compartments where it is a cofactor for the dioxygenases that hydroxylate the transcription factor HIF and trigger its degradation by VHL. Since HIF turns on oncogenic pathways, IDH3 has apparent tumor suppressor activity. Two isoforms of the human protein are produced by alternative splicing.

Protein type: Mitochondrial; Carbohydrate Metabolism - citrate (TCA) cycle; Oxidoreductase; EC 1.1.1.41

Chromosomal Location of Human Ortholog: 20p13

Cellular Component: mitochondrial matrix; mitochondrion; nucleus

Molecular Function: electron carrier activity; isocitrate dehydrogenase (NAD+) activity; magnesium ion binding; NAD binding

Biological Process: 2-oxoglutarate metabolic process; cellular metabolic process; isocitrate metabolic process; NADH metabolic process; tricarboxylic acid cycle

Disease: Retinitis Pigmentosa 46