Analytical Data
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基因名
ospA
- Application
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别名
ospA;TIL4;Toll-like receptor 2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q5SDL7
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表达区间
1-161aa
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氨基酸序列
MVAMEAMAAMEVMVAAMAATADTVASSAASATATEATVAMDTASLSLPLQLSPRSLPQSSLSATAATVATDTVVSSADTEVSDTEDSAATVSATASLSMLPQSSPRSLPQSSLSATAATVDSVTDMADTAMDTKQFISKGNEHFFAASYLCAWADQSAAGS
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分子量
20.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.












