Recombinant OmpA protein (Tagged) is a Haemophilus influenzae Full Length protein, in the 22 to 359 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
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Acts as a fimbriae subunit, allowing adhesion to host cells. With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.
ompP5, ompA, Outer membrane protein P5, OMP P5, Fimbrin, Outer membrane porin A, Outer membrane protein A
Recombinant OmpA protein (Tagged) is a Haemophilus influenzae Full Length protein, in the 22 to 359 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Acts as a fimbriae subunit, allowing adhesion to host cells.
Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpA family.
OmpA also known as Outer Membrane Protein A is a significant membrane protein found in many Gram-negative bacteria including Escherichia coli (E. coli). It has a molecular mass of approximately 35 kDa. This protein is expressed in the outer membrane of these bacterial cells. The structure of OmpA includes a beta-barrel that enables it to function as a channel for the passage of small molecules. Its stability and role in maintaining membrane integrity make it an important element of bacterial survival.
OmpA plays a critical role in interactions between the bacterial cell and its environment. It is involved in cell adhesion and invasion influencing the bacterium's ability to establish infection. This protein does not typically exist as part of a larger complex yet it contributes to the structural and functional roles of the bacterial outer membrane. Furthermore it aids in the stabilization of the outer membrane by interacting with other components including lipopolysaccharides.
OmpA is integral to bacterial nutrient uptake mechanisms and the response to environmental changes. It participates in the pathway for porin-mediated transport which includes proteins like FepA another outer membrane protein involved in iron transport. Through its channel-forming properties OmpA influences the diffusion of small molecules and ions underlining its involvement in vital processes of cellular homeostasis and response to oxidative stress.
OmpA is connected to infectious diseases caused by pathogenic E. coli strains and other Gram-negative bacteria. It serves as a virulence factor contributing to pathogenicity by facilitating the invasion of host cells and evading the immune response. Diseases related to these bacteria such as urinary tract infections (UTIs) demonstrate the importance of OmpA in pathogenicity. OmpA also has connections to proteins like TLR2 (Toll-Like Receptor 2) which recognizes bacterial components and activates immune cell responses linking OmpA to inflammation and immune system modulation.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis of ab226269 with 5% enrichment gel and 15% separation gel.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS analysis result of ab226269 could indicate that this peptide derived from E.coli-expressed Haemophilus influenzae ompA.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS analysis result of ab226269 could indicate that this peptide derived from E.coli-expressed Haemophilus influenzae ompA.
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