Analytical Data
-
基因名
xynG1
- Application
-
别名
Endo-1,4-beta-xylanase; Paenibacillus sp. 7541; Glycosidase; Hydrolase; 3.2.1.8
-
种属
Others
-
表达系统
E. coli
-
标签
Strep;His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
A0A269WC65
-
表达区间
A29-R366
-
蛋白长度
Full Length of Mature Protein
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
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.












