Analytical Data
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Gene name
Nitrilase
- Application
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Alternative Names
Alcaligenes sp. EGD-AK7; Hydrolase
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Species
Human
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
U7U7F7
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Expression Region
M1-S356
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Protein Length
Full Length
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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
Nitrilase is an important biocatalyst that plays a crucial role in the biodegradation of nitriles, which are environmental pollutants, as well as in the synthesis of value-added chemicals in organic synthesis. These enzymes, belonging to the family of amidases, are capable of hydrolyzing nitriles into their corresponding carboxylic acids and ammonia, thus providing a more environmentally friendly alternative to traditional chemical processes. The production of nitrilase through recombinant DNA technology has gained significant attention due to its potential for enhanced catalytic efficiency and specificity. Researchers have focused on cloning the nitrilase genes from various microorganisms, optimizing expression systems, and characterizing the enzymatic properties of the resulting recombinant proteins. This enables insights into the enzyme's mechanisms and substrate specificity, as well as its application in bioremediation and biotransformations. The exploration of nitrilase has further implications in pharmaceuticals and agriculture, where these enzymes can be used in the synthesis of biologically active compounds and the detoxification of harmful chemicals. Overall, the study of recombinant nitrilase proteins holds great promise for sustainable development and green chemistry applications.
