Cart (0 Items)
Your cart is currently empty.
View ProductsSize | 100ug |
---|---|
Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Pseudomonas aeruginosa PcrV Protein, N-His & N-SUMO |
---|---|
Origin species | Pseudomonas aeruginosa |
Expression system | Prokaryotic expression |
Molecular weight | 30.43 kDa |
Buffer | 0.01M PBS, pH 7.4. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Leu132-Ile294 |
Aliases /Synonyms | Type III secretion protein PcrV, pcrV, PA1706 |
Reference | ARO-P12724 |
Note | For research use only. |
The Recombinant Pseudomonas aeruginosa PcrV protein is a key component of the type III secretion system (T3SS) in the Gram-negative bacterium Pseudomonas aeruginosa. This protein is a highly conserved antigen that plays a crucial role in the pathogenesis of P. aeruginosa infections. In this article, we will discuss the structure, activity, and potential applications of the Recombinant Pseudomonas aeruginosa PcrV protein.
The PcrV protein is a 30 kDa protein that is composed of 294 amino acids. It is a highly stable protein that forms a homodimer in solution. The crystal structure of the PcrV protein has been determined and it consists of two domains – an N-terminal α-helical domain and a C-terminal β-barrel domain. The α-helical domain is responsible for protein-protein interactions, while the β-barrel domain is involved in pore formation. The PcrV protein also contains a hydrophobic patch that is essential for its membrane localization and function.
The PcrV protein is a key component of the T3SS, which is a specialized secretion system used by P. aeruginosa to deliver effector proteins into host cells. The T3SS is essential for the virulence of P. aeruginosa and the PcrV protein is a major virulence factor. The PcrV protein is secreted by P. aeruginosa and forms a complex with other proteins, including PcrG and PopB/PopD, to form the translocon complex. This complex is responsible for the delivery of effector proteins into host cells.
The PcrV protein also has a pore-forming activity, which is essential for the secretion of effector proteins. It forms a pore in the host cell membrane, allowing the effector proteins to pass through and exert their effects. The PcrV protein has also been shown to have immunomodulatory effects, as it can inhibit the activation of host immune cells and promote bacterial survival.
The PcrV protein has been extensively studied for its potential as a vaccine candidate against P. aeruginosa infections. Recombinant PcrV protein has been shown to induce protective immune responses in animal models, making it a promising candidate for a P. aeruginosa vaccine. In fact, a recombinant PcrV-based vaccine has been developed and is currently in clinical trials for the prevention of P. aeruginosa infections in high-risk populations, such as cystic fibrosis patients.
In addition to its potential as a vaccine candidate, the PcrV protein has also been studied for its use in diagnostic tests for P. aeruginosa infections. Antibodies against PcrV have been shown to be highly specific for P. aeruginosa and can be used in diagnostic assays to detect the presence of the bacteria in clinical samples.
Furthermore, the PcrV protein has been investigated as a potential target for novel therapeutics against P. aeruginosa infections. Inhibitors of the PcrV protein have been developed that can block its pore-forming activity and inhibit the secretion of effector proteins, thus reducing the virulence of P. aeruginosa. These inhibitors have shown promising results in animal models and may lead to the development of new treatments for P. aeruginosa infections.
The Recombinant Pseudomonas aeruginosa PcrV protein is a key virulence factor and potential vaccine candidate for P. aeruginosa infections. Its structure and activity have been extensively studied, and it has shown promising results in various applications, including as
Send us a message from the form below
Reviews
There are no reviews yet.