Analytical Data
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Gene name
dspB
- Application
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Alternative Names
(Beta-N-acetylhexosaminidase)(Fragment)
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Species
Aggregatibacter actinomycetemcomitans
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q840G9
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Expression Region
1-361aa
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Molecular Weight
48.4 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
The study of recombinant DSPB protein is grounded in the increasing interest in bioactive peptides and their therapeutic potential. DSPB, derived from the bacterium *Halobacillus halophilus*, has garnered attention due to its unique structure and functional properties that may have applications in biotechnology and medicine. Research has highlighted its role in cellular processes, particularly in the modulation of immune responses and its antimicrobial activities. As antibiotic resistance becomes a global health concern, the development of alternative therapeutics that leverage natural proteins like DSPB is crucial. Moreover, advances in recombinant DNA technology have enabled the efficient expression and purification of DSPB in various host systems, facilitating detailed studies of its biological activities. Investigating the structure-function relationships of DSPB can provide insights into its mechanisms of action, paving the way for novel drug designs and therapeutic strategies. Thus, the exploration of DSPB as a recombinant protein is not only significant for academic research but also holds promise for practical applications in healthcare and industry.
