Analytical Data
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Gene name
flaA
- Application
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Alternative Names
flaA;CARD12;CLAN;CLAN1;NLR family CARD domain-containing Protein 4
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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
Q46113
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Expression Region
2-575aa
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AA Sequence
GFRINTNVAALNAKANADLNSKSLDASLSRLSSGLRINSAADDASGMAIKDSLRSQANTLGQAISNGNDALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLMEELDNIANTTSFNGKQLLSGNFINQEFQIGASSNQTVKASIGATQSSKIGLTRFETGSRISVGGEVQFTLKNYNGIDDFKFQKVVISTSVGTGLGALADEINKNADKTGVRATFTVETRGMGAVRAGATSDDFAINGVKIGKVDYKDGDANGALVSAINSVKDTTGVEASIDENGKLLLTSREGRGIKIEGNIGRGAFINPNMLENYGRLSLVKNDGKDILISGTNLSAIGFGTGNMISQASVSLRESKGQIDANVADAMGFNSANKGNILGGYSSVSAYMSSTGSGFSSGSGFSVGSGKNYSTGFANTIAISAASQLSAVYNVSAGSGFSSGSNLSQFATMKTSAGNTLGVKDETAGVTTLKGAMAVMDIAETAITNLDQIRADIGSVQNQVTSTINNITVTQVNVKAAESQIRDVDFAAESANYSKANILAQSGSYAMAQANSVQQNVLRLLQ
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Molecular Weight
60.4 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
FlaA, a flagellin protein, is a crucial component of the bacterial flagellum, playing a significant role in motility and host-pathogen interactions. The study of FlaA recombinant protein has gained attention due to its potential applications in vaccine development and immunology. Flagellin is known to act as an endotoxin, eliciting strong immune responses, making it a target for therapeutic interventions against various bacterial infections. By producing FlaA in a recombinant form, researchers aim to investigate its structural properties, immune response profile, and role in bacterial virulence. Understanding the mechanisms by which FlaA modulates host immune responses can provide insights into the design of novel vaccines and treatments. Moreover, studying the recombinant FlaA protein can help elucidate its interactions with immune receptors, such as Toll-like receptor 5 (TLR5), enhancing our knowledge of pathogen recognition and the subsequent immune activation pathways. Overall, the research on FlaA recombinant protein is pivotal not only for advancing our understanding of bacterial pathogenesis but also for developing innovative strategies to combat infectious diseases.











