Tricarboxylate transport Recombinant Protein | SLC20A3 recombinant protein

Recombinant Human Tricarboxylate transport protein

Cat. Num. AAA717193

• Gene Names: SLC25A1; CTP; SEA; D2L2AD; SLC20A3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Tricarboxylate transport; Recombinant Human Tricarboxylate transport protein; Citrate transport protein; CTP; Solute carrier family 25 member 1; Tricarboxylate carrier protein; SLC20A3 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: 47-87aa; Partial
• Sequence: EYVKTQLQLDERSHPPRYRGIGDCVRQTVRSHGVLGLYRGL
• Sequence Length: 311

• 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 SLC20A3 recombinant protein

Involved in citrate-H+/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD+ for the glycolytic pathway.

Product Categories/Family for SLC20A3 recombinant protein

Transport

References

Localization of the human mitochondrial citrate transporter protein gene to chromosome 22q11 in the DiGeorge syndrome critical region.Heisterkamp N., Mulder M.P., Langeveld A., ten Hoeve J., Wang Z., Roe B., Groffen J.Genomics 29:451-456(1995) Cloning, genomic organization, and chromosomal localization of human citrate transport protein to the DiGeorge/velocardiofacial syndrome minimal critical region.Goldmuntz E., Wang Z., Roe B.A., Budarf M.L.Genomics 33:271-276(1996) 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) 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) 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) Deficiency in SLC25A1, encoding the mitochondrial citrate carrier, causes combined D-2- and L-2-hydroxyglutaric aciduria.Nota B., Struys E.A., Pop A., Jansen E.E., Fernandez Ojeda M.R., Kanhai W.A., Kranendijk M., van Dooren S.J., Bevova M.R., Sistermans E.A., Nieuwint A.W., Barth M., Ben-Omran T., Hoffmann G.F., de Lonlay P., McDonald M.T., Meberg A., Muntau A.C., Nuoffer J.M., Parini R., Read M.H., Renneberg A., Santer R., Strahleck T., van Schaftingen E., van der Knaap M.S., Jakobs C., Salomons G.S.Am. J. Hum. Genet. 92:627-631(2013)

NCBI and Uniprot Product Information

• NCBI GeneID: 6576
• UniProt Accession #: P53007; Q9BSK6; A8K8E8
• Molecular Weight: 31.8 kDa
• NCBI Official Synonym Full Names: solute carrier family 25 (mitochondrial carrier; citrate transporter), member 1
• NCBI Official Symbol: SLC25A1
• NCBI Official Synonym Symbols: CTP; SEA; D2L2AD; SLC20A3
• NCBI Protein Information: tricarboxylate transport protein, mitochondrial
• UniProt Protein Name: Tricarboxylate transport protein, mitochondrial
• Protein Family: Tricarboxylate transport protein
• UniProt Gene Name: SLC25A1
• UniProt Synonym Gene Names: SLC20A3; CTP
• UniProt Entry Name: TXTP_HUMAN

NCBI Description

This gene encodes a member of the mitochondrial carrier subfamily of solute carrier proteins. Members of this family include nuclear-encoded transporters that translocate small metabolites across the mitochondrial membrane. This protein regulates the movement of citrate across the inner membranes of the mitochondria. Mutations in this gene have been associated with combined D-2- and L-2-hydroxyglutaric aciduria. Pseudogenes of this gene have been identified on chromosomes 7, 11, 16, and 19. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2013]

Uniprot Description

SLC25A1: Involved in citrate-H(+)/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway. Belongs to the mitochondrial carrier family.

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

Chromosomal Location of Human Ortholog: 22q11.21

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

Molecular Function: citrate transmembrane transporter activity; structural constituent of ribosome

Biological Process: carbohydrate metabolic process; cellular lipid metabolic process; citrate transport; gluconeogenesis; glucose metabolic process; translation; transmembrane transport; triacylglycerol biosynthetic process

Disease: Combined D-2- And L-2-hydroxyglutaric Aciduria