Analytical Data
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Gene name
xynG1
- Application
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Alternative Names
Endo-1,4-beta-xylanase; Paenibacillus sp. 7541; Glycosidase; Hydrolase; 3.2.1.8
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Species
Others
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A269WC65
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Expression Region
A29-R366
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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
The study of the xynG1 recombinant protein is situated within the broader context of lignocellulosic biomass degradation, which is crucial for sustainable biofuel production and the valorization of agricultural residues. XynG1, a gene encoding endo-1,4-xylanase, is derived from certain microorganisms that possess the ability to efficiently break down xylan, a major component of hemicellulose in plant cell walls. The increasing interest in renewable energy sources has spurred research into enzymes that can enhance the breakdown of complex carbohydrates into fermentable sugars. Understanding the structure-function relationship of xynG1 can provide insights into its catalytic mechanism, substrate specificity, and potential applications in various industrial processes, such as paper and pulp industries, and the production of biorefineries. Moreover, the recombinant expression of xynG1 in suitable host systems allows for the production of this enzyme in high yields, facilitating its purification and functional characterization. The insights gained from xynG1 research not only contribute to fundamental enzyme science but also hold promise for improving the efficiency of biomass conversion processes, thus addressing global energy demands and environmental challenges.
