Analytical Data
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Gene name
disA
- Application
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Alternative Names
Cyclic di-AMP synthase (c-di-AMP synthase) (Diadenylate cyclase)
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Species
Mycobacterium paratuberculosis
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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
Q743W9
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Expression Region
1-357aa
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Molecular Weight
45.9 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
DisA is a crucial protein involved in the regulation of gene expression related to cellular responses in bacteria, particularly in relation to the SOS response and stress adaptation. The study of DisA has gained significance due to its role in maintaining genome stability and mediating the bacterial response to DNA damage. Research shows that DisA acts as a signaling molecule that detects DNA integrity and activates appropriate repair mechanisms, which helps bacteria survive under hostile conditions. Its unique function in sensing DNA topology and coordinating cellular responses has made it an attractive target for understanding bacterial resilience and pathogenicity. The structural and functional analysis of DisA, especially in model organisms like Bacillus subtilis, has provided insights into its mechanism of action and its potential interactions with other cellular components. Additionally, the potential for DisA to serve as a target for novel antimicrobial strategies highlights the importance of this protein in microbiological research. As antibiotic resistance continues to rise, understanding the role of DisA in bacterial survival mechanisms could lead to innovative approaches in the development of new therapeutics. Thus, ongoing investigations into the reconstitution and function of DisA not only contribute to fundamental microbiology but also pave the way for applied research in combating bacterial infections and enhancing our understanding of bacterial physiology and adaptability.
