Analytical Data
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Gene name
fliA
- Application
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Alternative Names
fliA;flaD;rpoF;RNA polymerase sigma factor FliA
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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
P0AEM6
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Expression Region
1-239aa
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AA Sequence
MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVERYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAIGQLEQELGRNATETEVAERLGIDIADYRQMLLDTNNSQLFSYDEWREEHGDSIELVTDDHQRENPLQQLLDSNLRQRVMEAIETLPEREKLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL
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Molecular Weight
27.7 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
The study of the fliA gene, which encodes a sigma factor crucial for the regulation of flagellar biosynthesis in bacteria, has garnered significant attention in microbiological research. Flagella are essential for bacterial motility and are involved in various processes such as colonization, biofilm formation, and virulence. The fliA gene plays a pivotal role in the gene expression regulation of flagellar assembly and function. Understanding the molecular mechanisms through which fliA operates can provide insights into how bacteria adapt to their environments and respond to various stimuli. Furthermore, as antibiotic resistance continues to pose a significant threat to public health, exploring the role of fliA and its associated pathways may unveil potential therapeutic targets. Research into fliA recombinant proteins offers the opportunity to characterize its function and interactions in vitro, paving the way for advancements in biotechnology and synthetic biology applications, including the development of novel antimicrobial agents or vaccines. Additionally, fliA's role in bacterial pathogenicity underscores its importance in infectious disease research. By elucidating the biochemical properties and regulatory networks involving fliA, scientists can deepen their understanding of bacterial behavior and potentially contribute to the development of innovative approaches to combat bacterial infections. This underscores the importance of ongoing research into fliA and its recombinant protein forms, as they represent a key area of study within microbial genetics and a potential avenue for addressing critical challenges in medicine and environmental microbiology.











