Analytical Data
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Gene name
TLR2
- Application
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Alternative Names
Tlr2
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Species
Mouse
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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
Q9QUN7
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Expression Region
25-250aa
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AA Sequence
QESLSCDASGVCDGRSRSFTSIPSGLTAAMKSLDLSFNKITYIGHGDLRACANLQVLILKSSRINTIEGDAFYSLGSLEHLDLSDNHLSSLSSSWF GPLSSLKYLNLMGNPYQTLGVTSLFPNLTNLQTLRIGNVETFSEIRRIDFAGLTSLNELEIKALSLRNYQSQSLKSIRDIHHLTLHLSESAFLLEI FADILSSVRYLELRDTNLARFQFSPLPVDEVSSP
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Molecular Weight
29 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
Protein Description
Toll-like receptor 2 (TLR2) is a crucial component of the innate immune system, playing a significant role in pathogen recognition and the activation of immune responses. TLR2 is known to recognize a wide variety of microbial components, including lipoproteins and peptidoglycan from bacteria, as well as certain fungal and viral elements, which makes it essential for the detection of various infectious agents. Research on recombinant TLR2 proteins has gained momentum due to their potential applications in vaccine development and immunotherapy. By producing TLR2 in a recombinant form, researchers can better understand its structural and functional characteristics, investigate its signaling pathways, and identify its interactions with other immune molecules. Additionally, recombinant TLR2 proteins can be used as immunological reagents to enhance immune responses in experimental models and may serve as therapeutic targets for modulating immune responses in conditions such as infections, autoimmune diseases, and cancer. As the field advances, the exploration of TLR2’s role in disease pathology and its therapeutic implications continues to be a significant area of investigation, with the potential to contribute to novel strategies for infection prevention and treatment.











