Recombinant Human TUFM protein (His tag) is a Human Full Length protein, in the 44 to 452 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Also plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy.
EF-Tu, P43, TUFM
Recombinant Human TUFM protein (His tag) is a Human Full Length protein, in the 44 to 452 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Also plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
TUFM also known as elongation factor Tu mitochondrial (EF-Tu) is a protein involved in the protein synthesis process within mitochondria. It has a molecular mass of approximately 50 kDa. TUFM plays an essential role in the translation step of protein synthesis by binding aminoacyl-tRNA and positioning it on the ribosome. Researchers have identified the protein as highly expressed in tissues with high energy demand such as the heart brain and skeletal muscle.
TUFM assists in mitochondrial protein synthesis which is necessary for the proper function and maintenance of the respiratory chain complexes. It forms part of the mitochondrial ribosome complex operating alongside other elongation factors like EF-G. TUFM’s activity is essential for the production of proteins encoded by mitochondrial DNA which are they key components of oxidative phosphorylation machinery.
TUFM integrates into the mitochondrial translation pathway which supports the production of proteins critical for the electron transport chain. This pathway is important for ATP production through oxidative phosphorylation. TUFM interacts with other components such as MRPS18 and MRPL3 to mediate the elongation cycle during mitochondrial protein synthesis. These relationships are essential for coordinating mitochondrial function and bioenergetics.
TUFM mutations or disruptions have connections to mitochondrial disorders such as MELAS syndrome (Mitochondrial Encephalomyopathy Lactic Acidosis and Stroke-like episodes) which affects energy production. The protein's dysfunction can also relate to Parkinson's Disease where impaired mitochondrial activity plays a role. TUFM’s interaction with other mitochondrial proteins like NDUFS1 part of complex I of the electron transport chain underlines its potential impact in these disorders.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab236184.
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