Recombinant Human Elongation Factor Tu, Mitochondrial (TUFM) Protein (His-SUMO)

Name: Recombinant Human Elongation Factor Tu, Mitochondrial (TUFM) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08624P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Elongation Factor Tu, Mitochondrial (TUFM) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P49411
Target Symbol	TUFM
Synonyms	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)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG
Expression Range	47-455aa
Protein Length	Full Length of Mature Protein
Mol. Weight	61.0kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Mitochondrion.
Protein Families	TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
Database References	HGNC: 12420 OMIM: 602389 KEGG: hsa:7284 STRING: 9606.ENSP00000322439 UniGene: 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.