Elongation factor Tu (TUFM) Recombinant Protein | TUFM recombinant protein

Recombinant Human Elongation factor Tu, mitochondrial (TUFM)

Cat. Num. AAA949820

• Gene Names: TUFM; P43; EFTU; COXPD4; EF-TuMT
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Elongation factor Tu (TUFM); Recombinant Human Elongation factor Tu; mitochondrial (TUFM); P43; TUFM 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: 44-452. Full Length of Mature Protein
• Sequence: AVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG

• 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 TUFM recombinant protein

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

Product Categories/Family for TUFM recombinant protein

Metabolism

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 34147630
• NCBI GeneID: 7284
• NCBI Accession #: NP_003312.3
• NCBI GenBank Nucleotide #: NM_003321.4
• UniProt Accession #: P49411; O15276
• Molecular Weight: 47 kDa
• NCBI Official Full Name: elongation factor Tu, mitochondrial
• NCBI Official Synonym Full Names: Tu translation elongation factor, mitochondrial
• NCBI Official Symbol: TUFM
• NCBI Official Synonym Symbols: P43; EFTU; COXPD4; EF-TuMT
• NCBI Protein Information: elongation factor Tu, mitochondrial
• UniProt Protein Name: Elongation factor Tu, mitochondrial
• UniProt Gene Name: TUFM
• UniProt Synonym Gene Names: EF-Tu
• UniProt Entry Name: EFTU_HUMAN

NCBI Description

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]

Uniprot Description

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