Analytical Data
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Gene name
tir
- Application
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Alternative Names
Secreted effector protein Tir
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
C6UYL8
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Expression Region
252-362aa
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Molecular Weight
27.8 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
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Protein Description
TIR (Toll/interleukin-1 receptor) domain-containing proteins play a crucial role in mediating immune responses and cellular signaling pathways. Their involvement in pathogen recognition and activation of downstream signaling cascades has made them a focal point of research in immunology and therapeutic development. Initially identified in plants, TIR domains have since been recognized in a variety of organisms, including animals and fungi, underscoring their evolutionary importance in innate immunity. The ability of TIR proteins to form complex networks in signal transduction is particularly significant in the context of innate immune receptor interactions, especially in response to viral and bacterial infections. Understanding the structure and function of TIR domain-containing proteins facilitates insights into their roles in inflammatory processes and potential dysregulation in autoimmune diseases. Moreover, the study of TIR protein engineering has opened avenues for developing novel therapeutic strategies, such as TIR domain-based immunomodulators. Recent advances in recombinant DNA technology and protein expression systems have enabled researchers to produce and analyze TIR proteins, providing valuable data on their function and interactions. As research continues to uncover the complexities of TIR protein signaling, it holds promise for harnessing these pathways for innovative treatments against infectious diseases and inflammatory disorders, thereby contributing to the ongoing quest for targeted and effective therapies in immunology.
