Analytical Data
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基因名
sacC
- Application
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别名
Beta-D-fructofuranosidase;Exo-beta-D-fructosidase;Exo-levanase
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种属
Bacillus subtilis
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P05656
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表达区间
25-677aa
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分子量
77.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
