Analytical Data
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Gene name
fla
- Application
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Alternative Names
41 kDa antigen;P41
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Species
Borrelia burgdorferi
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11089
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Expression Region
1-336aa
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Molecular Weight
51.8 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
Fla (flagellar) proteins are integral components of the bacterial flagellar apparatus, playing a crucial role in motility and pathogenesis. These proteins, particularly FlaA in many Gram-negative bacteria, are essential for the assembly and function of flagella, which are whip-like structures that enable bacteria to swim through liquid environments. Research into Fla proteins has gained considerable interest due to their implications in bacterial behavior and infection mechanisms. For instance, flagella are often associated with the virulence of pathogenic bacteria, facilitating adherence to host tissues and evasion of the immune response. Moreover, studies have shown that the structural and functional properties of Fla proteins can vary significantly across different species, highlighting their evolutionary significance. Understanding the molecular mechanisms underlying Fla protein assembly and regulation not only enhances our knowledge of bacterial mobility but also opens potential avenues for the development of novel therapeutic strategies aimed at disrupting bacterial motility and reducing infection rates. As antibiotic resistance continues to rise, targeting flagellar proteins presents a promising approach in the ongoing battle against bacterial infections. Thus, research on Fla proteins represents a vital intersection of microbiology, molecular biology, and medical science, driving efforts towards innovative solutions for public health challenges.











