Recombinant Pseudomonas aeruginosa PcrV Protein, N-His from ProteoGenix; catalogue ARO-P10831; research use only.
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Pseudomonas aeruginosa is a gram-negative bacterium that is commonly found in the environment and can cause infections in humans. One of the virulence factors of this bacterium is the PcrV protein, which is a key component of the type III secretion system (T3SS). This protein is essential for the bacterium to cause disease and has been identified as a potential target for vaccine development. In recent years, recombinant Pseudomonas aeruginosa PcrV protein has been extensively studied for its structure, activity, and application in various fields.
The PcrV protein is a highly conserved protein among different strains of Pseudomonas aeruginosa. It is a 33 kDa protein that is composed of 294 amino acids. The protein is divided into three domains: N-terminal, central, and C-terminal. The N-terminal domain is responsible for binding to the T3SS needle, while the central domain is involved in the formation of the T3SS translocon. The C-terminal domain is responsible for binding to the host cell receptor, which is crucial for the delivery of effector proteins into the host cell.
Recombinant Pseudomonas aeruginosa PcrV protein is produced by cloning the gene encoding for the protein into a suitable expression vector and then expressing it in a host organism such as Escherichia coli. The protein is then purified using various techniques such as affinity chromatography, ion exchange chromatography, and size exclusion chromatography. The purified protein is highly stable and retains its structural integrity, making it an ideal candidate for further studies.
The PcrV protein is a key component of the T3SS, which is a complex machinery used by Pseudomonas aeruginosa to inject effector proteins into host cells. The PcrV protein plays a crucial role in the assembly and function of the T3SS translocon, which is responsible for forming a pore in the host cell membrane for the delivery of effector proteins. Additionally, the PcrV protein also interacts with the host cell receptor, facilitating the delivery of effector proteins into the host cell.
Recombinant Pseudomonas aeruginosa PcrV protein has been shown to retain its activity and functionality, making it a valuable tool for studying the role of this protein in the pathogenesis of Pseudomonas aeruginosa. It has also been used in various in vitro and in vivo studies to understand the mechanism of action of the T3SS and to identify potential therapeutic targets.
The PcrV protein has been identified as a potential vaccine candidate for Pseudomonas aeruginosa infections. Recombinant Pseudomonas aeruginosa PcrV protein has been used in various studies to develop vaccines that can induce a protective immune response against Pseudomonas aeruginosa infections. These vaccines have shown promising results in animal models and are currently being tested in clinical trials.
Apart from its potential as a vaccine candidate, recombinant Pseudomonas aeruginosa PcrV protein has also been used in the development of diagnostic tools for Pseudomonas aeruginosa infections. The protein has been used in immunoassays to detect the presence of Pseudomonas aeruginosa in clinical samples, providing a rapid and accurate method for diagnosis.
In addition, recombinant Pseudomonas aeruginosa PcrV protein has also been studied for its potential as a therapeutic target. Inhibitors targeting the PcrV protein have shown promising results in reducing the virulence of Pseudomonas aeruginosa and increasing the efficacy of antibiotics in treating infections caused by this bacterium.
In conclusion,
ProteoGenix catalogue number ARO-P10831. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 20.20 kDa; Fragment: Leu132-Ile294; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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