Analytical Data
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Gene name
yopB
- Application
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Alternative Names
yopB；yopB；Type 3 secretion system translocon Protein SctE
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Species
E.coli
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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
P37131
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Expression Region
1-401aa
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AA Sequence
MSALITHDRSTPVTGSLVPYIETPAPAPLQTQQVAGELKDKNGGVSSQGVQLPAPLAVVASQVTEGQQQEITKLLESVTRGTAGSQLISNYVSVLTNFTLASPDTFEIELGKLVSNLEEVRKDIKIADIQRLHEQNMKKIEENQEKIKETEENAKQVKKSGMASKIFGWLIAIASVVIGAIMVASGVGAVAGAMMIASGVIGMANMAVKQAAEDGLISQEAMQVLGPILTAIEVALTVVSTVMTFGGSALKCLADIGAKLGANTASLAAKGAEFSAKVAQISTGISNTVGSAVTKLGGSFGSLTMSHVIRTGSQATQVAVGVGSGITQTINNKKQADLQHNNADLALNKADMAALQSIIDRLKEELSHLSESHRQVMELIFQMINAKGDMLHNLAGRPHTV
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Molecular Weight
41.9 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
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.
