Analytical Data
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Gene name
sacC
- Application
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Alternative Names
Beta-D-fructofuranosidase;Exo-beta-D-fructosidase;Exo-levanase
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Species
Bacillus subtilis
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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
P05656
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Expression Region
25-677aa
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Molecular Weight
77.2 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
SacC, a secreted amylase from the bacterium *Bacillus subtilis*, plays a pivotal role in starch degradation, making it an attractive target for research in biotechnology and molecular biology. As an enzyme that catalyzes the hydrolysis of starch and related polysaccharides into simpler sugars, SacC has applications in various industries, including food, textile, and biofuel production. The study of recombinantly expressed SacC protein allows for the exploration of its enzymatic properties, stability, and potential modifications that could enhance its activity or specificity. Furthermore, understanding the structure-function relationship of SacC through recombinant expression and characterization may lead to improvements in industrial processes, such as more efficient starch processing or the development of novel biocatalysts. Additionally, this research contributes to the broader field of enzyme engineering, where insights gained from studying SacC can inspire the design of tailor-made enzymes for specific applications. Thus, investigating the recombinant production and functional analysis of SacC not only sheds light on its biochemical pathways but also holds significant promise for advancing industrial biotechnology.
