Analytical Data
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Gene name
marA
- Application
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Alternative Names
/
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Species
Shigella sonnei
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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
Q3Z1R7
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Expression Region
1-129aa
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Molecular Weight
22.9 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
The MarA protein, a transcriptional regulator in Escherichia coli, is a key player in the bacterial response to environmental stresses, including antibiotic exposure and oxidative stress. As a member of the AraC/XylS family of regulator proteins, MarA can activate a variety of genes associated with multidrug resistance, leading to an efflux of antibiotics and enhancing bacterial survival under adverse conditions. Research into MarA has gained momentum due to the global rise of antibiotic resistance, posing a significant threat to public health. Investigating the mechanisms by which MarA regulates its target genes provides insights into the development of effective strategies to combat resistant pathogens. Recent studies have focused on the structural and functional characterization of MarA, employing techniques such as X-ray crystallography and mutagenesis, which have revealed how MarA recognizes specific DNA sequences and interacts with other proteins. Understanding these interactions at a molecular level is crucial for the design of inhibitors that could disrupt MarA's function and possibly restore the efficacy of existing antibiotics. Overall, the study of MarA not only contributes to the fundamental understanding of gene regulation in bacteria but also has potential implications for innovative approaches in antimicrobial therapy.
