Analytical Data
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Gene name
tbpA
- Application
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Alternative Names
(TbpA)(Transferrin-binding protein 1)
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Species
Haemophilus influenzae
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P44970
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Expression Region
24-912aa
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Molecular Weight
102.9 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 research on the tbpA recombinant protein is rooted in the need for understanding the TbpA protein's role in the pathogenesis of pathogenic bacteria, particularly in relation to human infections. TbpA, or transferrin-binding protein A, is crucial for iron acquisition, a vital process for bacterial survival and virulence. Many pathogens, such as Neisseria meningitidis and Haemophilus influenzae, rely on TbpA to capture iron from the host's transferrin, thereby facilitating their growth and infection. The study of tbpA has significant implications for developing novel therapeutic strategies, as targeting this protein could potentially disrupt iron acquisition and limit bacterial proliferation. Furthermore, recombinant forms of TbpA can be synthesized for use in vaccine development, aiming to elicit an immune response that can protect against these infections. Advancements in recombinant DNA technology have enabled researchers to produce large quantities of tbpA, allowing for detailed investigations into its structure, function, and interaction with host immune components. Understanding the mechanisms by which tbpA operates not only elucidates the fundamental biology of pathogenic bacteria but also holds promise for innovative approaches to combat bacterial infections, ultimately contributing to improved human health outcomes.
