Analytical Data
-
Gene name
cobB
- Application
-
Alternative Names
Regulatory protein SIR2 homolog
-
Species
strain B100
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
B0RM75
-
Expression Region
1-293aa
-
Molecular Weight
48.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 cobB recombinant protein is situated in the context of understanding the biochemical pathways involved in bacterial metabolism and virulence. CobB, a nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, is crucial for the regulation of the cellular acetylation status, influencing various cellular processes, including gene expression and energy metabolism in bacteria. It is particularly notable in the model organism *Escherichia coli*, where it plays a role in the deacetylation of target proteins, thereby impacting their functions and interactions. Research has shown that CobB is involved in the regulation of virulence factors, suggesting its potential role in the pathogenicity of certain bacteria. Additionally, studying this enzyme can provide insights into its function in diverse physiological contexts, including stress responses and adaptation mechanisms. The recombinant production of CobB facilitates detailed characterization of its enzymatic activity and interaction with other cellular components. By generating CobB as a recombinant protein, researchers can explore its structure-function relationships, enzymatic kinetics, and inhibition, potentially paving the way for novel antibacterial strategies. Understanding the role of CobB in bacterial cells can contribute to broader applications in microbiology and biotechnology, offering avenues for developing treatments against bacterial infections or enhancing industrial fermentation processes.
