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AB274655

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

Key facts

Tags

Tag free

Applications

SDS-PAGE, ELISA

applications

Biologically active

No

Accession

P04977

Animal free

No

Carrier free

No

Species

Bordetella pertussis Tohama I

Storage buffer

pH: 8 Constituents: 50% Glycerol (glycerin, glycerine), 47.1% Tris HCl, 2.9% Sodium chloride

storage-buffer

Reactivity data

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Product details

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.

Sequence info

[{"sequence":"","proteinLength":null,"predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Native","expressionSystem":null,"accessionNumber":null,"tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
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.

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.

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.

Product protocols

Target data

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.
See full target information ptxA

Additional targets

ptxD,ptxB,ptxC,ptxE,ptxA

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