Analytical Data
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Gene name
Cutinase
- Application
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Alternative Names
(Cutin hydrolase)
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Species
Magnaporthe oryzae
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Source
Yeast
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30272
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Expression Region
17-228aa
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Molecular Weight
24.1 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
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.
