Analytical Data
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Gene name
XYLB
- Application
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Alternative Names
XYLB; Xylulose kinase; Xylulokinase; EC 2.7.1.17
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75191
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Expression Region
1-536 aa
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AA Sequence
MAEHAPRRCCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKLEQRILSQTRGPPE
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Molecular Weight
84.8 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
XYLB, a recombinant protein derived from the xylanase family, plays a pivotal role in the degradation of hemicellulose, a major component of plant cell walls. The study of XYLB is significant in various fields, particularly in biotechnology and biofuels, as it can enhance the efficiency of biomass conversion processes. With the growing global focus on renewable energy sources and the need for sustainable agricultural practices, understanding and optimizing XYLB's enzymatic properties is crucial for the development of eco-friendly methods to transform lignocellulosic biomass into fermentable sugars. Furthermore, recombinant DNA technology allows for the production of XYLB in various host systems, which facilitates its large-scale application in industries such as paper, textiles, and animal feed. Research into XYLB not only aims to improve its activity and stability under industrial conditions but also explores its potential synergistic effects with other enzymes, paving the way for novel enzymatic cocktails that can significantly boost biomass degradation. Additionally, characterizing the structure-function relationship of XYLB can provide insights into its mechanistic pathways and guide future engineering efforts to create more efficient variants. Overall, the exploration of XYLB as a recombinant protein underlines the intersection of molecular biology, environmental science, and industrial applications, highlighting its relevance in addressing contemporary challenges related to energy and resource sustainability.











