Analytical Data
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Gene name
bglIIM
- Application
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Alternative Names
N(4)- cytosine-specific methyltransferase BglII
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Species
Bacillus subtilis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q45489
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Expression Region
1-360aa
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Molecular Weight
58 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
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Protein Description
BglIIM is a unique and intriguing recombinant protein derived from the bacterium Bacillus licheniformis, known for its role in the degradation of aromatic compounds. This protein is classified as a glycosyltransferase, which is essential for catalyzing the transfer of sugar moieties to various substrates, thus having significant implications in both industrial and environmental applications. The study of BglIIM is particularly relevant in the context of biomass conversion and bioremediation, where its ability to modify carbohydrates can enhance the efficiency of biofuel production and the degradation of complex pollutants. Furthermore, the understanding of its structure and function can lead to advancements in biotechnology, such as the development of novel enzymes that are more efficient or have altered specificity for targeted reactions. Recent research has focused on the recombinant expression of BglIIM in different host systems to optimize its yield and functionality for practical applications. Investigating the catalytic mechanisms and substrate specificity of this protein not only contributes to fundamental knowledge in enzymology but also opens up avenues for engineering new biocatalysts with improved performance in various industrial processes.
