Succinyl-CoA ligase [GDP-forming] subunit beta Recombinant Protein | SUCLG2 recombinant protein

Recombinant Human Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial

Cat. Num. AAA1350641

• Gene Names: SUCLG2; GBETA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Succinyl-CoA ligase [GDP-forming] subunit beta; Recombinant Human Succinyl-CoA ligase [GDP-forming] subunit beta; mitochondrial; GTP-specific succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase beta-G chain; SCS-betaG; SUCLG2 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: 49-423aa; Partial
• Sequence: MSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLEDAAK

• 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 SUCLG2 recombinant protein

Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA.

Product Categories/Family for SUCLG2 recombinant protein

Metabolism

References

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, annotation and analysis of human chromosome 3.Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.Nature 440:1194-1198(2006) Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes.Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.J. Biol. Chem. 273:27580-27586(1998) Mei G., Yu W., Gibbs R.A. 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)

NCBI and Uniprot Product Information

• NCBI GI #: 294862256
• NCBI GeneID: 8801
• NCBI Accession #: NP_001171070.1
• NCBI GenBank Nucleotide #: NM_001177599.1
• UniProt Accession #: Q96I99; O95195; Q6NUH7; Q86VX8; Q8WUQ1; C9JVT2
• Molecular Weight: 56.3 kDa
• NCBI Official Full Name: succinyl-CoA ligase
• NCBI Official Synonym Full Names: succinate-CoA ligase, GDP-forming, beta subunit
• NCBI Official Symbol: SUCLG2
• NCBI Official Synonym Symbols: GBETA
• NCBI Protein Information: succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
• UniProt Protein Name: Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
• Protein Family: Succinate--CoA ligase
• UniProt Gene Name: SUCLG2
• UniProt Synonym Gene Names: SCS-betaG
• UniProt Entry Name: SUCB2_HUMAN

NCBI Description

This gene encodes a GTP-specific beta subunit of succinyl-CoA synthetase. Succinyl-CoA synthetase catalyzes the reversible reaction involving the formation of succinyl-CoA and succinate. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are found on chromosomes 5 and 12. [provided by RefSeq, Apr 2010]

Uniprot Description

SUCLG2: Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA. Belongs to the succinate/malate CoA ligase beta subunit family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Carbohydrate Metabolism - propanoate; Carbohydrate Metabolism - citrate (TCA) cycle; Mitochondrial; EC 6.2.1.4; Ligase

Chromosomal Location of Human Ortholog: 3p14.1

Cellular Component: microtubule organizing center; mitochondrial matrix; mitochondrion; nucleus; plasma membrane

Molecular Function: ATP binding; GTP binding; succinate-CoA ligase (GDP-forming) activity

Biological Process: cellular metabolic process; succinyl-CoA metabolic process; tricarboxylic acid cycle