Native Bordetella pertussis toxin/ptxD protein
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Native Bordetella pertussis toxin/ptxD protein is a Bordetella pertussis Tohama I protein, suitable for SDS-PAGE, ELISA.
View Alternative Names
BP3783, ptxA, Pertussis toxin subunit 1, PTX S1, Islet-activating protein S1, NAD-dependent ADP-ribosyltransferase, IAP S1
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Pertussis toxin disrupts host immune responses and cellular signaling pathways. It is an important component of the ab5 toxin family where one A subunit and five B subunits form a complex to enter cells. The toxin binds to cell surface glycoproteins facilitating its uptake and subsequent inhibition of G-protein-coupled receptor (GPCR) signaling. This action interferes with a variety of intracellular processes ultimately leading to altered immune regulation and enhanced bacterial colonization.
Pathways
Pertussis toxin plays a significant role in the intracellular signaling pathways especially impacting the GPCR pathways. The toxin's catalytic subunit modifies the alpha subunit of inhibitory G-proteins (Gi) which prevents normal signal transduction from the GPCRs. This dysregulation impairs processes such as cyclic AMP (cAMP) regulation and immune response modulation. In the GPCR pathway B. pertussis toxin shows close functional relationships with other G-protein coupled components.
Specifications
Form
Liquid
Additional notes
This product is highly purified from Bordetella pertussis culture supernatant.
General info
Function
S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD(+) into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors.
Sequence similarities
Belongs to the bacterial exotoxin subunit A family.
Target data
Additional targets
Product promise
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