Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

TUFM

Uniprot No.

P49411

Research Area

Epigenetics and Nuclear Signaling

Alternative Names

COXPD4; EF Tu; EF TuMT; EF-Tu; EF-TuMT; EFTu; EFTU_HUMAN; EFTuMT; Elongation factor Tu; Elongation factor Tu mitochondrial; mitochondrial; P43; Tu translation elongation factor; mitochondrial; Tufm

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

47-455aa

Target Protein Sequence

AVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

49.0 kDa

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

Tris-based buffer,50% glycerol

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Target Background

Function

Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays also a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIG-I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy.

Gene References into Functions

Novel mutation in mitochondrial Elongation Factor EF-Tu associated to dysplastic leukoencephalopathy and defective mitochondrial DNA translation. PMID: 28132884
study revealed a novel role for TUFM as a host restriction factor that exerts an inhibitory effect on avian-signature PB2627E influenza virus propagation in human cells; found that increased TUFM-dependent autophagy correlates with the inhibitory effect on avian-signature influenza virus replication and may serve as a key intrinsic mechanism to restrict avian influenza virus infection in humans PMID: 28611246
High expression of TUFM is associated with colorectal cancer. PMID: 28449687
we identify a novel signaling hub centering on the NLRX1 TUFM protein complex, promoting autophagic flux. Defects in the expression of either NLRX1 or TUFM result in compromised autophagy when treated with EGFR inhibitors.These findings expand our understanding of the components involved in head and neck squamous cell carcinoma autophagy machinery that responds to EGFR inhibitors. PMID: 26876213
TUFM is a novel regulator of epithelial-mesenchymal transition (EMT); there may be a molecular link between mitochondrial dysfunction and EMT induction PMID: 26781467
NLRX1 and TUFM work in concert to reduce cytokine response and augment autophagy. PMID: 23321557
Increased expression of TUFM is a promising new prognostic indicator for colorectal carcinoma. PMID: 22772342
By recruiting Atg5-Atg12 and NLRX1, TUFM serves as a nodal checkpoint of the RIG-I-MAVS axis. It acts similarly to NLRX1 by inhibiting RigI-like-receptor-induced IFN-I but promoting autophagy. PMID: 22749352
Genetic investigation of patients with defective mitochondrial translation led to the discovery of novel mutations in the mitochondrial elongation factor G1 (EFG1) in one affected baby and in the mitochondrial elongation factor Tu (EFTu) in another one PMID: 17160893
Myoblasts isolated from the MELAS patients show A3243G mutation in tRNALeu(UUR) produces a severe respiratory chain deficiency and this phenotype can be partially suppressed by overexpression of EFTu and EFG2. PMID: 18753147
Results suggest that the R336Q mutant mt-EFTu variant fails to bind to aminoacylated mitochondrial tRNAs, thus explaining the observed impairment of mitochondrial translation. PMID: 19524667

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Involvement in disease

Combined oxidative phosphorylation deficiency 4 (COXPD4)

Subcellular Location

Mitochondrion.

Protein Families

TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily

Database Links

HGNC: 12420

OMIM: 602389

KEGG: hsa:7284

STRING: 9606.ENSP00000322439

UniGene: Hs.12084

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Code	CSB-EP025342HUa0
MSDS	MSDS
Size	$224
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human Elongation factor Tu, mitochondrial (TUFM)

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