Analytical Data
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Gene name
iutA
- Application
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Alternative Names
(Cloacin receptor)
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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
P14542
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Expression Region
26-732aa
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Molecular Weight
85.5 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 iutA gene encodes the outer membrane receptor protein for iron-regulated uptake in various pathogenic bacteria, particularly in Escherichia coli. Understanding iutA and its corresponding recombinant protein has become crucial due to its role in iron acquisition, which is vital for bacterial growth and virulence, especially under iron-limited conditions common in host environments. As iron is an essential nutrient that is often sequestered by host defenses, bacteria have evolved sophisticated mechanisms to capture and utilize it. The study of iutA recombinant protein helps elucidate the molecular mechanisms of iron transport and the interactions with siderophores, small iron-chelating compounds secreted by bacteria. Moreover, insights gained from iutA research can pave the way for the development of new antibacterial strategies, particularly as drug resistance becomes an increasing concern. Understanding the structural and functional properties of iutA recombinant protein can also contribute to vaccine development and the design of novel therapeutic agents targeting iron acquisition pathways. Thus, the investigation of iutA recombinant protein is of significant interest not only for its biological implications but also for its potential applications in combating bacterial infections.
