Analytical Data
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Gene name
Tlr11
- Application
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Alternative Names
Toll-like receptor 12
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6R5P0
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Expression Region
769-926aa
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Molecular Weight
25.7 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
Toll-like receptor 11 (TLR11) is a pivotal component of the innate immune system, primarily recognized for its role in detecting pathogens and initiating immune responses. Research on TLR11 has gained significance due to its involvement in recognizing specific microbial components, particularly those from protozoan parasites like Toxoplasma gondii and Schistosoma mansoni. Unlike other TLRs, TLR11 is primarily expressed in the kidney and is crucial for the activation of dendritic cells and the subsequent production of pro-inflammatory cytokines. The study of recombinant TLR11 proteins has become essential for elucidating its signaling mechanisms and functional characteristics. By producing TLR11 in a recombinant form, researchers can investigate its ligand-binding properties, identify potential therapeutic targets, and develop strategies for enhancing immune responses. Additionally, understanding TLR11's molecular structure and interactions with pathogens could lead to advancements in vaccine development and improved treatments for diseases caused by TLR11 ligands. This research context highlights the importance of TLR11 in immunology and opens up avenues for innovative therapeutic interventions.
