Recombinant P.IB (porB) protein (Tagged) is a Neisseria meningitidis H44/76 Full Length protein, in the 20 to 331 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
NMBH4476_1982, NMH_2035, porB, Major outer membrane protein P.IB, PIB, Protein IB, Class 3 protein, Porin
Recombinant P.IB (porB) protein (Tagged) is a Neisseria meningitidis H44/76 Full Length protein, in the 20 to 331 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Serves as a slightly cation selective porin.
Belongs to the Gram-negative porin family.
The protein P.IB also referred to as porB or porB/hup is a part of the porin family found in the outer membrane of the bacteria Neisseria gonorrhoeae and Neisseria meningitidis. These porins form channels that allow the passage of small molecules and ions across the membrane. PorB has an approximate molecular mass of 34 kDa and plays an important role in bacterial cell permeability. Its expression is tightly regulated and highly relevant to the survival mechanisms of Neisseria species.
Porins like P.IB are critical in the exchange of nutrients and waste products across the bacterial membrane. P.IB being part of a pore-forming complex enables these bacteria to adapt to various environmental conditions by controlling the flow of ions and small molecules. The structural arrangement of P.IB aids in interactions with the host immune system impacting pathogenesis and immune evasion. Therefore the presence of P.IB in Neisseria enhances its adaptability and virulence.
P.IB interacts significantly in bacterial pathways governing membrane transport. It plays a role in metabolism and ion regulation ensuring the bacteria's survival in diverse environments. Its interaction with human immune system components makes it a target for studying evasion pathways. P.IB is related to other Neisseria porins like PorA and together these proteins facilitate essential processes that are necessary for maintaining bacterial homeostasis.
P.IB is most commonly associated with conditions like gonorrhea and meningococcal meningitis. Its presence in the outer membrane is linked to increased invasiveness of Neisseria gonorrhoeae and Neisseria meningitidis infections. The pathogenic role of P.IB has been connected to its interaction with host proteins and immune defenses emphasizing its importance in studying bacterial virulence and developing treatments. These interactions make P.IB an appealing target for research aiming to develop interventions against these bacterial infections.
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