Analytical Data
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Gene name
iagB
- Application
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Alternative Names
iagB; STM2877Invasion protein IagB
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Species
Salmonella typhimurium
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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
P0CL15
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Expression Region
20-160aa
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Molecular Weight
32 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
IagB, a protein found in certain pathogenic bacteria, plays a crucial role in the regulation of virulence and pathogenicity. Research on IagB has gained attention due to its involvement in bacterial responses to environmental stresses, which can influence infectious processes. Its function is linked to the modulation of bacterial signaling pathways, particularly those related to the type III secretion system (T3SS), a key mechanism through which many bacteria inject effector proteins into host cells, facilitating infection. Understanding the structure and function of IagB is essential for unraveling the molecular mechanisms of bacterial virulence. Additionally, IagB represents a potential target for novel therapeutic strategies aimed at combating bacterial infections, as inhibiting its activity could weaken the virulence of pathogenic strains. Advances in recombinant protein technology allow for the production and characterization of IagB, enabling detailed studies of its biochemical properties and interactions with other cellular components. Consequently, IagB not only serves as a significant focus of study within microbiology and infectious diseases but also holds promise for informing the development of innovative antimicrobial agents. As researchers continue to elucidate the various roles of IagB within pathogenic bacteria, it may contribute to the broader understanding of bacterial adaptation and survival strategies in hostile environments.
