Analytical Data
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Gene name
TLR1
- Application
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Alternative Names
TLR1；KIAA0012；Toll-like receptor 1
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Species
Human
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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
Q15399
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Expression Region
25-580aa
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AA Sequence
SEFLVDRSKNGLIHVPKDLSQKTTILNISQNYISELWTSDILSLSKLRILIISHNRIQYLDISVFKFNQELEYLDLSHNKLVKISCHPTVNLKHLDLSFNAFDALPICKEFGNMSQLKFLGLSTTHLEKSSVLPIAHLNISKVLLVLGETYGEKEDPEGLQDFNTESLHIVFPTNKEFHFILDVSVKTVANLELSNIKCVLEDNKCSYFLSILAKLQTNPKLSNLTLNNIETTWNSFIRILQLVWHTTVWYFSISNVKLQGQLDFRDFDYSGTSLKALSIHQVVSDVFGFPQSYIYEIFSNMNIKNFTVSGTRMVHMLCPSKISPFLHLDFSNNLLTDTVFENCGHLTELETLILQMNQLKELSKIAEMTTQMKSLQQLDISQNSVSYDEKKGDCSWTKSLLSLNMSSNILTDTIFRCLPPRIKVLDLHSNKIKSIPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELGEFVKNIDQVSSEVLEGWPDSYKCDYPESYRGTLLKDFHMSELSCNIT
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Molecular Weight
65.2kDa
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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
TLR1 (Toll-Like Receptor 1) is a crucial component of the innate immune system, playing a pivotal role in the detection of microbial pathogens. It forms a heterodimer with TLR2, facilitating the recognition of various lipid-based antigens, particularly from Gram-positive bacteria and certain fungi. Research into TLR1 recombinant protein has significantly increased due to its potential applications in vaccine development and immunotherapy. Understanding the structural and functional characteristics of TLR1 can aid in deciphering its mechanism of action in pathogen recognition and subsequent immune response activation. Moreover, the elucidation of TLR1’s signaling pathways can provide insights into its role in inflammatory diseases and autoimmune disorders. Recombinant TLR1 proteins are utilized in various studies to investigate their interactions with ligands and assess their immunogenicity. These studies are vital for developing strategies to enhance host defenses against infections and for engineering adjuvants that can potentiate vaccine efficacy. The advancement of recombinant DNA technology has facilitated the production of TLR1 proteins, allowing for the detailed analysis of their biochemical properties and biological functions. This research is essential for therapeutic applications, including autoimmune diseases, where modulation of TLR1 activity may offer new treatment avenues. The knowledge gained from TLR1 recombinant protein studies not only contributes to basic immunological understanding but also holds promise for translational advancements in clinical immunotherapy and vaccine design. In summary, TLR1 recombinant protein research represents a significant frontier in immunology, with the potential to inform and transform therapeutic approaches against infectious and inflammatory diseases.
