Analytical Data
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Gene name
LCC
- Application
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Alternative Names
Leaf-branch compost cutinase; LC-cutinase; LCC; PET-digesting enzyme; Poly(ethylene terephthalate) hydrolase; PET hydrolase; PETase
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
G9BY57
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Expression Region
S36-Q293
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Protein Length
Full Length of Mature Protein
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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
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.
