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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Staphylococcus aureus lukF-PV Protein, N-His |
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Origin species | Staphylococcus aureus |
Expression system | Prokaryotic expression |
Molecular weight | 36.60 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
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 | Ala25-Ser325 |
Aliases /Synonyms | Panton-Valentine bi-component leukocidin subunit F; lukF-PV |
Reference | ARO-P11747 |
Note | For research use only. |
Recombinant proteins have revolutionized the field of biotechnology and have become essential tools in various scientific applications. One such protein is the Recombinant Staphylococcus aureus lukF-PV Protein, which has gained significant attention due to its potential role as an antigen in vaccine development against Staphylococcus aureus infections.
The lukF-PV gene encodes for the LukF-PV protein, which belongs to the family of pore-forming toxins known as the staphylococcal leukotoxins. The recombinant form of this protein is produced by cloning the lukF-PV gene into an expression vector and expressing it in a suitable host organism, such as Escherichia coli.
The recombinant LukF-PV protein is composed of 296 amino acids and has a molecular weight of approximately 34 kDa. It has a similar structure to its native form, with a three-domain structure consisting of a hydrophobic N-terminal domain, a central beta-barrel domain, and a C-terminal alpha-helical domain. This structure is crucial for the protein’s function as it allows it to form pores in the cell membrane of target cells.
The main activity of the LukF-PV protein is its ability to form pores in the cell membrane of target cells, leading to cell lysis and death. This protein is specifically active against human and rabbit polymorphonuclear leukocytes, which are immune cells involved in fighting bacterial infections.
The formation of pores by LukF-PV protein is a multistep process that involves binding to specific receptors on the target cell membrane, oligomerization, and insertion of the beta-barrel domain into the membrane, ultimately leading to pore formation. This activity is crucial for the virulence of Staphylococcus aureus, as it allows the bacteria to evade the host’s immune response and cause tissue damage.
The unique structure and activity of the LukF-PV protein make it a promising candidate for various scientific applications. One of the most significant applications of this protein is its potential use as an antigen in vaccine development against Staphylococcus aureus infections.
Staphylococcus aureus is a major cause of both community and hospital-acquired infections, and the increasing prevalence of antibiotic-resistant strains has highlighted the need for alternative treatment strategies. Vaccines targeting the LukF-PV protein have shown promising results in preclinical studies, with the potential to provide protection against a wide range of Staphylococcus aureus strains.
In addition to its use in vaccine development, recombinant LukF-PV protein has also been used in diagnostic assays for the detection of Staphylococcus aureus infections. The protein’s ability to specifically target polymorphonuclear leukocytes makes it a valuable tool for identifying and differentiating Staphylococcus aureus from other bacterial infections.
In conclusion, the Recombinant Staphylococcus aureus lukF-PV Protein is a structurally and functionally important protein with potential applications in vaccine development and diagnostic assays. Its unique structure and activity make it a promising candidate for targeting Staphylococcus aureus infections, which continue to pose a significant threat to human health. Further research and development of this protein are necessary to fully utilize its potential in the fight against Staphylococcus aureus infections.
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