Analytical Data
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Gene name
disA
- Application
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Alternative Names
disA；DNA integrity scanning Protein DisA
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MTRPTLRETVARLAPGTGLRDGLERILRGRTGALIVLGNDENVEAICDGGFALDVRYAPTRLRELAKMDGAVVLSTDGSRIVRANVQLVPDPSIATDESGTRHRSAERAAIQTGYPVISVSHSMNIVTVYVGGERHVVADSATILSRANQAIATLERYKIRLDEVSRQLSRAEIEDFVTLRDVLTVVQRLELVRRIGQVIDNDVVELGTDGRQLRLQLDELLGGNDNARELIVRDYHASPEQLSEAQMTATLDELDALSDTELLDFTALAKVFGYPTTTEAQDSAVSPRGYRALAGIPRLQFAHADLLVRSFGTLQNVLAASASDLQSIDGIGAMWARHVREGLSQLAESTITDSLS
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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 protein that plays a crucial role in bacterial signal transduction, specifically in the regulation of the stringent response in organisms such as Bacillus subtilis. Understanding the mechanisms of DisA is important because it links the perception of nutritional stress to the synthesis of the alarmone (p)ppGpp, which modulates various cellular processes, including metabolism, growth, and virulence. The study of DisA involves examining its structural and functional properties, revealing how it senses changes in the intracellular levels of nucleotide pools and translates these signals into appropriate cellular responses. Research has shown that DisA interacts with other proteins and can form oligomers, suggesting a complex regulatory network. Additionally, the insights gained from DisA studies not only enhance our knowledge of bacterial physiology but also have potential applications in developing antibacterial strategies by targeting this regulatory pathway, making it an attractive focus for both fundamental and applied microbiological research. As antibiotic resistance continues to pose a global threat, unraveling the roles of proteins like DisA could lead to innovative therapeutic approaches that disrupt bacterial survival mechanisms.
