Analytical Data
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基因名
Cutinase
- Application
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别名
(Cutin hydrolase)
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种属
Magnaporthe oryzae
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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
P30272
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表达区间
17-228aa
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分子量
28.5 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
Cutinases are a group of enzymes that play a crucial role in the degradation of cutin, a natural polymer found in the plant cuticle. They have garnered significant attention in recent years due to their potential applications in various fields, including agriculture, biotechnology, and environmental science. The increasing interest in sustainable practices has highlighted the need for effective biocatalysts that can facilitate the breakdown of plant biomass, making cutinases valuable for biofuel production and waste management. Moreover, the ability of cutinases to degrade synthetic polymers, such as polyethylene terephthalate (PET), has opened new avenues for addressing plastic pollution. The recombinant production of cutinases allows for enhanced yields and improved enzyme properties, facilitating detailed studies on their mechanisms of action and optimizing their use in industrial processes. Research in this area focuses on cloning and expressing cutinase genes in suitable host systems, such as bacteria or yeast, to produce large quantities of active enzyme for characterization and application. Understanding the structure-function relationship of these enzymes also aids in the design of engineered variants with tailored properties for specific industrial needs. As the demand for eco-friendly solutions continues to rise, the study of recombinant cutinases remains at the forefront of research aimed at harnessing microbial enzymes for sustainable development.












