Analytical Data
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Gene name
lcrV
- Application
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Alternative Names
lcrV；Virulence-associated V antigen
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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
P23994
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Expression Region
1-326aa
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AA Sequence
MIRAYEQNPQHFIEDLEKVRVEQLTGHGSSVLEELVQLVKDKNIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVIHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSGGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQEGETEKKIVSIKNFLESEKKRTGALGNLKDSYSYNKDNNELSHFATTCSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDDTSGK
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Molecular Weight
37.3 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
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Protein Description
The LcrV protein, a key virulence factor of the pathogenic bacterium Yersinia pestis, plays a critical role in the bacteria's ability to evade the host immune system. As a lipoprotein, LcrV is essential for the assembly and function of the type III secretion system (T3SS), which enables Y. pestis to deliver effector proteins directly into host cells, thereby facilitating infection and immune evasion. Research has increasingly focused on the potential of LcrV as a vaccine candidate due to its immunogenic properties, which can elicit strong immune responses in vaccinated hosts. Additionally, studies have shown that LcrV is conserved among various Yersinia species, heightening its significance not only for understanding Y. pestis pathogenesis but also for devising broad-spectrum vaccines against Yersinia infections. Recombinant LcrV protein has been produced in various expression systems, allowing for detailed structural and functional analyses. These investigations aim to elucidate the protein's mechanisms of action and its interactions with host immune components. By exploring the immunological responses triggered by LcrV, researchers are uncovering the protein's potential as a crucial target for therapeutic interventions and vaccine development against plague and related Yersinia diseases. Given the historical impact of Y. pestis as a causative agent of plague pandemics, ongoing research into the LcrV protein not only contributes to our understanding of bacterial pathogenesis but also has significant public health implications in terms of prevention and control strategies against this deadly pathogen.
