Analytical Data
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Gene name
TLR5
- Application
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Alternative Names
TLR5；TIL3；Toll-like receptor 5
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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
O60602
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Expression Region
640-858aa
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AA Sequence
FSLFIVCTVTLTLFLMTILTVTKFRGFCFICYKTAQRLVFKDHPQGTEPDMYKYDAYLCFSSKDFTWVQNALLKHLDTQYSDQNRFNLCFEERDFVPGENRIANIQDAIWNSRKIVCLVSRHFLRDGWCLEAFSYAQGRCLSDLNSALIMVVVGSLSQYQLMKHQSIRGFVQKQQYLRWPEDLQDVGWFLHKLSQQILKKEKEKKKDNNIPLQTVATIS
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Molecular Weight
26.5 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
Identification
Protein Description
TLR5 (Toll-like receptor 5) is a key component of the innate immune system, primarily recognized for its role in detecting bacterial flagellin, a crucial structural protein of bacterial flagella. The activation of TLR5 leads to the initiation of immune responses, thereby playing a pivotal role in the body's defense against bacterial infections. Recent studies have highlighted the significance of TLR5 not only in pathogen recognition but also in modulating inflammatory responses and influencing adaptive immunity. The recombinant protein form of TLR5 has garnered interest for its potential applications in vaccine development, as it can enhance the immune response when used as an adjuvant. Researchers are exploring the structural and functional characteristics of TLR5 recombinant proteins to better understand their mechanisms of action, optimize their immunogenicity, and evaluate their efficacy in therapeutic contexts. Moreover, the recombinant TLR5 protein is being investigated for its ability to stimulate potency against various pathogens, thereby presenting promising avenues for clinical applications in infectious diseases and immunotherapy. Understanding the functional dynamics of TLR5 through recombinant technology not only elucidates fundamental immunological processes but also opens doors for innovative strategies in disease prevention and treatment.
