Analytical Data
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Gene name
gspB
- Application
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Alternative Names
(Adhesin GspB)(Serine-rich adhesin for platelets)(Serine-rich repeat protein GspB)
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Species
Streptococcus gordonii
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q939N5
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Expression Region
233-617aa
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Molecular Weight
68.5 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
Recombinant GspB protein, derived from the pathogenic bacterium Streptococcus gordonii, has garnered significant attention in microbiological and immunological research due to its role in host-pathogen interactions. GspB is a glycoprotein that is expressed on the bacterial surface and is known to mediate adhesion to host tissues, contributing to biofilm formation and persistence in the oral cavity. Understanding the structure and function of GspB is critical for elucidating its mechanisms of pathogenicity and its interactions with host immune responses. Research has shown that GspB can bind to extracellular matrix proteins, such as fibronectin, and may thus facilitate bacterial colonization and infection. Additionally, due to its immunogenic properties, GspB is being investigated as a potential candidate for vaccine development against oral diseases, particularly periodontitis and endocarditis, which are associated with S. gordonii infection. The production of recombinant GspB allows for the detailed study of its functional properties, potential as a therapeutic target, and its role in immune evasion. Thus, the exploration of GspB not only enhances our understanding of bacterial pathogenesis but also opens avenues for innovative strategies in preventing and treating bacterial infections.
