Analytical Data
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Gene name
flgM
- Application
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Alternative Names
(Anti-sigma-28 factor)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AEM4
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Expression Region
1-97aa
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Molecular Weight
17.8 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
FlgM is a key regulatory protein involved in the flagellar biosynthesis and control of motility in many bacteria, particularly in species such as *Salmonella* and *Escherichia coli*. This protein acts as an anti-sigma factor that interacts with the sigma factor σ28, inhibiting its function until the flagellum is fully assembled. The regulation of flagellar assembly is critical for bacterial motility, allowing these organisms to adapt to various environments and evade immune responses. Given the increasing interest in bacterial motility as a potential target for new antimicrobial therapies, research focused on FlgM has gained momentum. Studies have aimed to elucidate the molecular mechanisms through which FlgM exerts its regulatory effects, its interactions with other flagellar components, and the conditions that trigger its activity. Understanding FlgM's role in flagellar assembly not only provides insights into bacterial physiology but also opens avenues for the development of novel strategies to combat infections caused by motile pathogens. Furthermore, recombinant FlgM protein production has been leveraged for structural biology studies and high-throughput screening assays to identify compounds that can disrupt its function, potentially leading to new therapeutic agents that hinder bacterial motility and persistence.
