No services found
No Products found
100ug, 50ug
ProteoGenix
Recombinant Proteins
Escherichia coli (E. coli)
Elisa, WB
E. coli ArsR Nter FLAG and Cter His recombinant protein is a highly versatile protein that plays a crucial role in the regulation of arsenic resistance in E. coli bacteria. This protein has been extensively studied and its structure, activity and application have been well characterized. In this article, we will provide a detailed description of the E. coli ArsR Nter FLAG and Cter His recombinant protein, highlighting its importance as a potential drug target and its various applications.
The E. coli ArsR Nter FLAG and Cter His recombinant protein is a 15.6 kDa protein consisting of 139 amino acids. It is a homodimer, with each monomer containing a DNA-binding domain and a metal-binding domain. The DNA-binding domain is responsible for the specific recognition and binding of the ArsR protein to the promoter region of the ars operon, which is involved in arsenic resistance. The metal-binding domain contains four cysteine residues that are essential for the binding of metal ions, particularly arsenite, which is the primary substrate of the ArsR protein.
The main function of the E. coli ArsR Nter FLAG and Cter His recombinant protein is to regulate the expression of genes involved in arsenic resistance. It acts as a transcriptional repressor, binding to the promoter region of the ars operon and preventing the expression of the ars genes. However, in the presence of arsenite, the ArsR protein undergoes a conformational change, leading to the dissociation of the protein from the DNA and subsequent activation of the ars genes. This allows the bacteria to develop resistance against arsenic by producing efflux pumps and enzymes that detoxify arsenic.
The E. coli ArsR Nter FLAG and Cter His recombinant protein has several applications, making it a valuable tool in both research and industrial settings. One of its major applications is in the development of new drugs targeting bacterial infections. As the ArsR protein is essential for the survival of E. coli, it is a potential drug target for the treatment of infections caused by this bacterium. Inhibitors of the ArsR protein could potentially disrupt the regulation of the ars operon and make the bacteria more susceptible to antibiotics.
In addition, the E. coli ArsR Nter FLAG and Cter His recombinant protein has been used in the development of biosensors for the detection of arsenic in environmental samples. By incorporating the ArsR protein into a biosensor, it is possible to detect even low concentrations of arsenic in water and soil samples. This has important implications for environmental monitoring and remediation.
Another potential application of the E. coli ArsR Nter FLAG and Cter His recombinant protein is in the field of bioremediation. As mentioned earlier, the ArsR protein is involved in the detoxification of arsenic in bacteria. By overexpressing this protein in bacteria, it is possible to enhance their ability to remove arsenic from contaminated environments. This has been demonstrated in several studies, where the ArsR protein was successfully used to improve the efficiency of arsenic bioremediation.
In summary, the E. coli ArsR Nter FLAG and Cter His recombinant protein is a crucial protein involved in the regulation of arsenic resistance in E. coli bacteria. Its structure, activity and various applications have been well characterized, making it a valuable tool in both research and industrial settings. With its potential as a drug target, biosensor component and bioremediation agent, this protein holds great promise for future advancements in the fields of medicine, environmental science and biotechnology.
Reviews
There are no reviews yet.
Your email address will not be published. Required fields are marked *
Your review *
Name *
Email *
Save my name, email, and website in this browser for the next time I comment.
Send us a message from the form below
First name
Last name
Email address
Lab / Company
Phone number
Message
send
Your cart is currently empty.