Analytical Data
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Gene name
lcrV
- Application
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Alternative Names
(Low calcium response locus protein V)
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Species
Yersinia pestis
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0C7U7
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Expression Region
1-326AA
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Molecular Weight
53.3 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
LcrV, a key component of the Yersinia pestis type III secretion system, plays a pivotal role in the virulence of this notorious pathogen, which is the causative agent of plague. As a multifunctional protein, LcrV is involved in modulating host immune responses and affecting the bacterial ability to invade host cells. Research on LcrV has gained momentum due to its potential as a vaccine candidate and therapeutic target against Yersinia infections. Its immunogenic properties make it a subject of interest for designing subunit vaccines that could elicit protective immune responses. Additionally, understanding the structural dynamics and functional mechanisms of LcrV can provide insights into the broader context of type III secretion systems across various pathogens. Structural studies, including crystallography and cryo-electron microscopy, have elucidated the protein's conformation and interactions, offering valuable data for rational drug design. The ongoing research efforts on LcrV involve exploring its role in bacterial pathogenesis, its interactions with host proteins, and the development of recombinant forms for vaccine trials, emphasizing the importance of this protein in the fight against infectious diseases caused by Yersinia species. Such studies not only contribute to our understanding of bacterial pathogenicity but also pave the way for innovative strategies in vaccine development and therapeutic interventions.
