Analytical Data
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基因名
yopB
- Application
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别名
yopB；yopB；Type 3 secretion system translocon Protein SctE
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种属
E.coli
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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
P37131
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表达区间
1-401aa
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氨基酸序列
MSALITHDRSTPVTGSLVPYIETPAPAPLQTQQVAGELKDKNGGVSSQGVQLPAPLAVVASQVTEGQQQEITKLLESVTRGTAGSQLISNYVSVLTNFTLASPDTFEIELGKLVSNLEEVRKDIKIADIQRLHEQNMKKIEENQEKIKETEENAKQVKKSGMASKIFGWLIAIASVVIGAIMVASGVGAVAGAMMIASGVIGMANMAVKQAAEDGLISQEAMQVLGPILTAIEVALTVVSTVMTFGGSALKCLADIGAKLGANTASLAAKGAEFSAKVAQISTGISNTVGSAVTKLGGSFGSLTMSHVIRTGSQATQVAVGVGSGITQTINNKKQADLQHNNADLALNKADMAALQSIIDRLKEELSHLSESHRQVMELIFQMINAKGDMLHNLAGRPHTV
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分子量
41.9 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
YopB is a virulence factor produced by Yersinia pestis, the bacterium responsible for plague, and Yersinia pseudotuberculosis. It functions as a part of the type III secretion system (T3SS), a mechanism that allows the bacterium to inject proteins directly into host cells, thereby subverting host immune responses. Understanding YopB's structure, function, and interactions with host cell machinery is critical for elucidating the pathogenicity of Yersinia species. Research on recombinant YopB protein has garnered significant interest because it serves as a potential target for vaccine development and therapeutic interventions. The production of this protein in recombinant systems facilitates the study of its immunogenic properties and its role in the context of infection. Furthermore, characterizing YopB can provide insights into the molecular mechanisms underlying bacterial invasion and immune evasion, which may lead to novel strategies for preventing or treating infections caused by these pathogens. Given the historical impact of plague and the continued relevance of Yersinia infections today, the study of YopB and its role in bacterial virulence is not only relevant for understanding disease mechanisms but also holds promise for advancing public health initiatives.
