Mitochondrial 2-oxoglutarate/malate carrier protein Recombinant Protein | SLC20A4 recombinant protein

Recombinant Human Mitochondrial 2-oxoglutarate/malate carrier protein

Cat. Num. AAA717341

• Gene Names: SLC25A11; OGC; SLC20A4
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Mitochondrial 2-oxoglutarate/malate carrier protein; Recombinant Human Mitochondrial 2-oxoglutarate/malate carrier protein; Solute carrier family 25 member 11; SLC20A4 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 43-82
• Sequence: DLVKNRMQLSGEGAKTREYKTSFHALTSILKAEGLRGIYT
• Sequence Length: 263

• 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 SLC20A4 recombinant protein

Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism.

Product Categories/Family for SLC20A4 recombinant protein

Transport

References

Sequences of the human and bovine genes for the mitochondrial 2-oxoglutarate carrier.Iacobazzi V., Palmieri F., Runswick M.J., Walker J.E.DNA Seq. 3:79-88(1992) Yu W., Gibbs R.A. DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.Nature 440:1045-1049(2006) Bienvenut W.V.Submitted (JUN-2005) to UniProtKB Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) 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) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) 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 GeneID: 8402
• UniProt Accession #: Q02978; O75537; Q969P7; F5GY65
• Molecular Weight: 31.9kD
• NCBI Official Synonym Full Names: solute carrier family 25 (mitochondrial carrier; oxoglutarate carrier), member 11
• NCBI Official Symbol: SLC25A11
• NCBI Official Synonym Symbols: OGC; SLC20A4
• NCBI Protein Information: mitochondrial 2-oxoglutarate/malate carrier protein
• UniProt Protein Name: Mitochondrial 2-oxoglutarate/malate carrier protein
• Protein Family: Mitochondrial 2-oxoglutarate/malate carrier protein
• UniProt Gene Name: SLC25A11
• UniProt Synonym Gene Names: SLC20A4; OGCP
• UniProt Entry Name: M2OM_HUMAN

NCBI Description

The oxoglutarate/malate carrier transports 2-oxoglutarate across the inner membranes of mitochondria in an electroneutral exchange for malate or other dicarboxylic acids (summary by Iacobazzi et al., 1992 [PubMed 1457818]).[supplied by OMIM, Jan 2011]

Uniprot Description

SLC25A11: Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism. Belongs to the mitochondrial carrier family.

Protein type: Transporter, SLC family; Membrane protein, multi-pass; Membrane protein, integral; Transporter; Mitochondrial

Chromosomal Location of Human Ortholog: 17p13.3

Cellular Component: integral to plasma membrane; mitochondrial inner membrane; mitochondrion; nucleus

Molecular Function: oxoglutarate:malate antiporter activity; structural constituent of ribosome

Biological Process: alpha-ketoglutarate transport; carbohydrate metabolic process; gluconeogenesis; glucose metabolic process; translation; transport