Analytical Data
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Gene name
tuf
- Application
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Alternative Names
tuf；FN；Fibronectin
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P99152
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Expression Region
1-394aa
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AA Sequence
MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKALEGDAQYEEKILELMEAVDTYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGLHDTSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTEFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVHLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIIK
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Molecular Weight
50.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
TUF (Translation Elongation Factor) proteins, specifically TUF-like proteins, play a critical role in protein synthesis as they are involved in the elongation phase of translation. Research has shown that TUF proteins are not only essential in various prokaryotic and eukaryotic organisms but also possess unique features that suggest their evolutionary significance. They are characterized by their ability to bind to aminoacyl-tRNA, facilitating the proper assembly of polypeptides during translation. Studies indicate that TUF proteins exhibit diverse functions beyond traditional roles in translation, including participation in cellular stress responses and regulation of gene expression. The investigation into TUF proteins is further propelled by their potential applications in biotechnology and medicine, particularly in developing novel therapeutic strategies against diseases linked to protein synthesis dysregulation, such as cancer and infections. Understanding the structural and functional dynamics of TUF proteins may also illuminate mechanisms of antibiotic resistance, as these proteins are targets for some antimicrobial agents. Overall, the research on TUF proteins is pivotal for unraveling the complexities of translational control and its implications for health and disease.
