Analytical Data
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Gene name
eglD
- Application
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Alternative Names
eglD；eglD；AA9 family lytic polysaccharide monooxygenase B
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96WQ9
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Expression Region
21-408aa
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AA Sequence
HTTVQAVWINGEDQGLGNTDDGYIRSPPSNSPVTDVTSTDMTCNVNGDQAASKTLSVKAGDVVTFEWHHSDRSDSDDIIASSHKGPVQVYMAPTAKGSNGNNWVKIAEDGYHKSSDEWATDILIANKGKHNITVPDVPAGNYLFRPEIIALHEGNREGGAQFYMECVQFKVTSDGSNELPSGVSIPGVYTATDPGILFDIYNSFDSYPIPGPDVWDGSSSGSSSSGSSSAAVSSAAAAATTSAVAATTPATQAAVEVSSSAAAATTEAAAPVVSSAAPVQQATSAVTSQAQAAPTTFATSSKKSSKTACKNKTKSNSQVAAATSSVVAPAATSSVVPVVSASASASAGGVAKQYERCGGINHTGPTTCESGSVCKKWNPYYYQCVASQ
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Molecular Weight
45.2 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
EglD, or Exopolygalacturonase D, is a key enzyme derived from the bacterium *Erwinia carotovora*, notable for its role in the degradation of pectin, a major component of plant cell walls. The interest in EglD research has surged due to its potential applications in agriculture, food processing, and biotechnological industries. As pectinases like EglD facilitate the softening of fruits and vegetables by breaking down pectin, understanding and manipulating this enzyme could lead to advancements in post-harvest technology, improving fruit storage and reducing spoilage. Furthermore, EglD's activity can enhance juice extraction processes, providing economic benefits in the beverage industry. On a broader scale, research into EglD also contributes to our understanding of plant-pathogen interactions, offering insights into how plant-infecting bacteria utilize pectin degradation to facilitate infection. The recombinant expression of EglD in microbial systems allows for the production of large quantities of the enzyme, paving the way for industrial applications. As researchers explore the structural and functional properties of EglD, including its substrate specificity and enzyme kinetics, they aim to engineer variants with improved efficacy and stability for specific applications. Overall, the study of EglD represents a vital intersection of plant biology, microbiology, and biotechnology, with significant implications for food science, agriculture, and environmental sustainability.
