Analytical Data
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Gene name
pgaB
- Application
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Alternative Names
(PGA N-deacetylase)(Poly-beta-1,6-GlcNAc N-deacetylase)
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Species
Escherichia coli
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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
P75906
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Expression Region
21-672aa
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Molecular Weight
82.6 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
PGA B recombinant protein has garnered significant attention in the fields of molecular biology and biotechnology due to its potential applications in various health and industrial processes. This protein is derived from the pathogenic bacterium *Clostridium perfringens*, which is known for its role in gastrointestinal diseases. The study of PGA B is vital because it has been implicated in bacterial adhesion and biofilm formation, processes crucial for infection establishment and persistence. By creating a recombinant version of this protein, researchers aim to better understand its structure-function relationships and the mechanisms underlying bacterial virulence. Additionally, PGA B has been explored for its potential use in vaccine development, as it may elicit an immune response that could provide protection against infections. The expression and purification of PGA B as a recombinant protein enable researchers to conduct detailed functional assays and structural analyses. Furthermore, insights gained from PGA B studies could contribute to the development of novel therapeutic strategies and diagnostic tools, addressing the growing concern of antibiotic resistance and enhancing our understanding of bacterial pathogenesis. Overall, the research surrounding PGA B recombinant protein represents a promising intersection of microbiology, immunology, and protein engineering, with implications for public health and disease management.
