protein

Recombinant Human Elongation factor Tu, mitochondrial

MBS949820

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Elongation factor Tu, mitochondrial

Elongation factor Tu

P43

elongation factor Tu, mitochondrial; Elongation factor Tu, mitochondrial; elongation factor Tu, mitochondrial; Tu translation elongation factor, mitochondrial; P43

TUFM

TUFM; TUFM; P43; EFTU; COXPD4; EF-TuMT; EF-Tu

EFTU_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

44-452

452

AVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILA
EGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARH
YAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQ
TREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEI
RELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQK
LLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTG
TLERGILKKGDECELLGHSKN

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Metabolism

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu.Woriax V.L., Burkhart W.A., Spremulli L.L.Biochim. Biophys. Acta 1264:347-356(1995) A mitochondrial elongation factor-like protein is over-expressed in tumours and differentially expressed in normal tissues.Wells J., Henkler F., Leversha M., Koshy R.FEBS Lett. 358:119-125(1995) The human mitochondrial elongation factor Tu (EF-Tu) gene cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene.Ling M., Merante F., Chen H.-S., Duff C., Duncan A.M.V., Robinson B.H.Gene 197:325-336(1997) The sequence and analysis of duplication-rich human chromosome 16.Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.Nature 432:988-994(2004) Dunn M.J.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) Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu.Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E., Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C., Comi G.P., Savasta S., Ferrero I., Zeviani M.Am. J. Hum. Genet. 80:44-58(2007)

34147630

NP_003312.3

NM_003321.4

P49411

61.02kD

Mitochondrial Translation Pathway (1268842); Mitochondrial Translation Elongation Pathway (1268844); Organelle Biogenesis And Maintenance Pathway (1268838)

This gene encodes a protein which participates in protein translation in mitochondria. Mutations in this gene have been associated with combined oxidative phosphorylation deficiency resulting in lactic acidosis and fatal encephalopathy. A pseudogene has been identified on chromosome 17. [provided by RefSeq, Jul 2008]

EFTU: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Defects in TUFM are the cause of combined oxidative phosphorylation deficiency type 4 (COXPD4). COXPD4 is characterized by neonatal lactic acidosis, rapidly progressive encephalopathy, severely decreased mitochondrial protein synthesis, and combined deficiency of mtDNA-related mitochondrial respiratory chain complexes. Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily. Protein type: Mitochondrial; RNA-binding; Translation; Translation elongation. Chromosomal Location of Human Ortholog: 16p11.2. Cellular Component: membrane; mitochondrion. Molecular Function: GTP binding; GTPase activity; protein binding; translation elongation factor activity. Biological Process: mitochondrial translation; organelle organization and biogenesis; translational elongation. Disease: Combined Oxidative Phosphorylation Deficiency 4

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750