Analytical Data
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Gene name
dapb2
- Application
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Alternative Names
Dipeptidyl aminopeptidase BII; dapb2; Pseudoxanthomonas mexicana; Aminopeptidase; Hydrolase; Protease
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Species
Others
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Source
E. coli
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Tag
His;Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
V5YM14
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Expression Region
G25-K722
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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
DapB2, a member of the D-amino acid oxidase family, has garnered significant attention in recent years due to its potential applications in various fields, including pharmacology, biotechnology, and bioremediation. This enzyme is known for its ability to catalyze the oxidative deamination of D-amino acids, which play critical roles in numerous biological processes, such as neurotransmission and microbial metabolism. The study of DapB2, particularly its recombinant form, allows researchers to explore its structural and functional properties in detail, paving the way for the development of novel biocatalysts and therapeutic agents. Additionally, understanding the mechanisms by which DapB2 interacts with substrates at the molecular level can provide valuable insights into enzyme engineering and metabolic engineering approaches. Furthermore, recombinant DapB2 serves as a model for investigating enzyme stability and activity in diverse environmental conditions, which is crucial for applications in industrial processes. As a result, research on DapB2 recombinant protein not only enhances our fundamental understanding of enzyme functionality but also holds promise for practical applications in sustainable technologies and drug development.
