Analytical Data
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Gene name
TR
- Application
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Alternative Names
TMEFF2; TENB2; HPP1; TPEF; CT120.2; Transmembrane Protein With EGF-Like And Two Follistatin-Like Domains 2; Hyperplastic polyposis protein 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UIK5
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Expression Region
Thr52~Arg290
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Molecular Weight
35kDa
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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
TR (Tetherin-resistant) recombinant proteins play a crucial role in virology and immunology research, particularly in the study of viral host interactions and immune evasion mechanisms. Tetherin, an antiviral protein expressed on the surface of infected cells, restricts the release of viral particles, including various enveloped viruses. Certain viruses, however, have developed strategies to counter this restriction. The understanding of TR recombinant proteins is vital for elucidating these viral resistance mechanisms, which can lead to the identification of potential therapeutic targets.
Research focusing on TR proteins includes their structure, function, and the molecular pathways they engage in to overcome tetherin-mediated restriction. Additionally, the development of TR recombinant proteins enables scientists to investigate their interactions with host factors and other viral proteins, providing insight into viral pathogenesis and the immune response. This research is particularly relevant for the design of novel antiviral therapies and vaccines, as it enhances our understanding of viral adaptation and resistance. Consequently, TR recombinant proteins serve as valuable tools in the ongoing effort to combat viral infections and improve public health outcomes.
