Native Bordetella pertussis toxin/ptxD protein is a Bordetella pertussis Tohama I protein and suitable for SDS-PAGE, ELISA.
Tag free
SDS-PAGE, ELISA
No
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes IgG and IgA ELISA Human |
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.
Pertussis toxin subunit 1, PTX S1, Islet-activating protein S1, NAD-dependent ADP-ribosyltransferase, IAP S1, BP3783, ptxA
Native Bordetella pertussis toxin/ptxD protein is a Bordetella pertussis Tohama I protein and suitable for SDS-PAGE, ELISA.
Pertussis toxin subunit 1, PTX S1, Islet-activating protein S1, NAD-dependent ADP-ribosyltransferase, IAP S1, BP3783, ptxA
Tag free
SDS-PAGE, ELISA
No
No
Bordetella pertussis Tohama I
pH: 8
Constituents: 50% Glycerol (glycerin, glycerine), 47.1% Tris HCl, 2.9% Sodium chloride
Liquid
This product is highly purified from Bordetella pertussis culture supernatant.
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.
Belongs to the bacterial exotoxin subunit A family.
Dry Ice
-80°C
Avoid freeze / thaw cycle
Sterility: Whole Bordetella pertussis organisms are removed by sterile filtration. Absence of viable B. Pertussis is confirmed negative by absence of growth under original culture conditions. Since no procedure can guarantee absolute sterility the reagent should be handled with appropriate safety precautions.
Bordetella pertussis toxin often called pertussis toxin or PTX functions mechanically as an exotoxin produced by Bordetella pertussis. This toxin has a molecular mass of around 105 kDa and comes from the bacterium responsible for whooping cough. It expresses itself in various host cells after the bacterium releases it into the respiratory tract during infection. The pertussis toxin consists of five subunits S1 through S5 which work together to impair host cellular functions by catalyzing the ADP-ribosylation of G-proteins.
Pertussis toxin disrupts host immune responses and cellular signaling pathways. It is an important component of the Anti-CENPF antibody 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.
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.
Pertussis toxin significantly contributes to the development of whooping cough a respiratory disease that can lead to severe coughing fits. This toxin affects various host immune proteins like chemokine receptors complicating immune response against the Bordetella pertussis bacterium. Additionally its action on the GPCR signaling pathway implicates it in other related respiratory conditions making pertussis toxin a pivotal target for therapeutic interventions and vaccine development against whooping cough.
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