Analytical Data
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Gene name
bgaC
- Application
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Species
Streptococcus pneumoniae
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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
A0A0T8M0L4
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Expression Region
1-595aa
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Molecular Weight
70.0 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
BgaC is a crucial enzyme involved in the hydrolysis of beta-glucans, polysaccharides found in various biological contexts, including plant cell walls and fungal structures. Research on BgaC recombinant protein has garnered significant attention due to its potential applications in biotechnology and food industries, particularly in processes that require the breakdown of complex carbohydrates. As the demand for sustainable methods of transforming biomass into fermentable sugars continues to rise, BgaC offers a promising biocatalytic solution. Understanding the structure and function of BgaC at the molecular level facilitates the development of more efficient, tailored enzymes for specific industrial applications. Moreover, advances in recombinant DNA technology have enabled the production of BgaC in host organisms, which enhances yield and facilitates downstream processing. Furthermore, studies on BgaC's substrate specificity and enzymatic mechanisms contribute to fundamental knowledge in enzymology and carbohydrate metabolism. As researchers strive to optimize BgaC for various applications, ongoing investigations aim to elucidate its biophysical properties, kinetics, and interactions with other biomolecules. This foundational research paves the way for the enzyme's innovative applications in biofuel production, bioremediation, and novel food processing technologies, ultimately promoting sustainable practices in multiple sectors.
