Analytical Data
-
基因名
marA
- Application
-
别名
/
-
种属
Shigella sonnei
-
表达系统
E. coli
-
标签
N- His & C- Myc
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q3Z1R7
-
表达区间
1-129aa
-
分子量
22.9 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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 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.












