Analytical Data
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Gene name
ospA
- Application
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Alternative Names
ospA；TIL4；Toll-like receptor 2
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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
Q5SDL7
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Expression Region
1-161aa
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AA Sequence
MVAMEAMAAMEVMVAAMAATADTVASSAASATATEATVAMDTASLSLPLQLSPRSLPQSSLSATAATVATDTVVSSADTEVSDTEDSAATVSATASLSMLPQSSPRSLPQSSLSATAATVDSVTDMADTAMDTKQFISKGNEHFFAASYLCAWADQSAAGS
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Molecular Weight
20.2 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
OspA (Outer Surface Protein A) is a critical antigen from the pathogenic bacterium Borrelia burgdorferi, which is the causative agent of Lyme disease. Research on OspA recombinant proteins has gained significant attention due to their potential application in vaccine development and immunodiagnostics. The recombinant expression of OspA allows for the production of large quantities of this protein, facilitating detailed studies on its structure, function, and immunogenicity. Understanding OspA's role in the pathogenesis of Lyme disease is essential, as it is involved in the initial interaction between the bacteria and the host immune system. Additionally, the ability to produce OspA in a recombinant form has opened avenues for the development of serological tests that can accurately detect Lyme disease in humans and animals. This is particularly important considering that early diagnosis and treatment are crucial for effective management of the disease. Furthermore, the characterization of OspA variants is vital for understanding the genetic diversity of Borrelia species and their potential impact on vaccine efficacy. Overall, the study of OspA recombinant proteins is pivotal not only for advancing our knowledge of Lyme disease pathogenesis but also for developing effective preventive measures and diagnostic tools.
