Analytical Data
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Gene name
fbpC
- Application
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Alternative Names
Acyl-CoA:diacylglycerol acyltransferase Antigen 85 complex C Short name: 85C Short name: Ag85C Fibronectin-binding protein C Short name: Fbps C
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Species
Mycobacterium tuberculosis
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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
P9WQN8
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Expression Region
46-340aa
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Molecular Weight
36.1 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
Recombinant FbpC protein, a member of the family of Fbp proteins, has gained attention in the field of molecular biology and immunology due to its potential role in pathogen interactions and immune response. FbpC, which stands for ferric binding protein C, is primarily known for its involvement in iron acquisition, a critical process for the survival and virulence of various bacteria. In many pathogenic organisms, FbpC contributes to the sequestration of iron from the host environment, which is essential for their growth and pathogenicity. The ability to produce recombinant FbpC allows researchers to study its structure and function in detail, facilitating the identification of its interaction with host factors and its role in bacterial infections. Moreover, FbpC's immunogenic properties make it a candidate for vaccine development, as it may elicit a protective immune response. Understanding the molecular mechanisms of FbpC not only aids in elucidating pathogenic strategies but also contributes to the development of novel therapeutic approaches against infectious diseases. The research surrounding recombinant FbpC protein is thus integral for advancing our knowledge of host-pathogen dynamics and for designing innovative interventions in infectious disease management.
