Analytical Data
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基因名
LCC
- Application
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别名
Leaf-branch compost cutinase; LC-cutinase; LCC; PET-digesting enzyme; Poly(ethylene terephthalate) hydrolase; PET hydrolase; PETase
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种属
Others
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表达系统
E. coli
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标签
N-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
G9BY57
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表达区间
S36-Q293
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蛋白长度
Full Length of Mature Protein
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分子量
29.9 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
Related Products
Protein Description
LCC (Lactose-Cleaving Component) recombinant proteins are increasingly significant in biotechnological applications, particularly in the dairy industry. As a valuable enzyme, LCC facilitates the hydrolysis of lactose into glucose and galactose, making dairy products more accessible to lactose-intolerant individuals. The rising awareness of lactose intolerance has led to a growing demand for lactose-free products, prompting extensive research into effective enzyme solutions. Traditional sources of LCC, such as microbial strains, have limitations in yield and efficiency. Therefore, recombinant DNA technology has emerged as a promising alternative, allowing for the expression of LCC in host organisms like bacteria, yeast, and plants, which can produce the enzyme in higher quantities and with tailored properties. This approach not only enhances the availability of lactose-free dairy but also enables the development of novel food products with improved digestibility and nutritional profiles. Moreover, research in this field explores optimizing LCC's enzymatic activity, stability, and production costs, making it a focal point of innovation in both food science and industrial enzyme applications. As such, the study of LCC recombinant proteins is pivotal in addressing consumer needs and advancing sustainable practices in food production.












