The PTXA Antibody (PACO34674) is a polyclonal antibody designed for researching PTXA, a toxin associated with the bacterium Bordetella pertussis, the causative agent of whooping cough. The antibody is produced in rabbits and is highly reactive with PTXA, making it an ideal tool for studying the toxin's role in pathogenesis and immune response.The PTXA Antibody has been validated for use in various applications, including ELISA and immunohistochemistry, allowing for accurate detection and localization of PTXA in samples. Its specificity for PTXA makes it a valuable tool for investigating the mechanisms by which this toxin contributes to the symptoms and progression of whooping cough.
Understanding the actions of PTXA is crucial for developing effective treatments and vaccines for whooping cough, a highly contagious respiratory disease that can be severe, especially in young children. Research using the PTXA Antibody can provide insights into how the toxin interacts with the host immune system and help identify potential targets for therapeutic interventions.
Antibody Name:
ptxA Antibody (PACO34674)
Antibody SKU:
PACO34674
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:1000-1:5000
Species Reactivity:
Bordetella pertussis
Immunogen:
Recombinant Bordetella pertussis Pertussis toxin subunit 1 protein (35-269AA)
Western blot. All lanes: Bordella pertussis pertussis toxin subunit 1 antibody at 2µg/ml + recombinant Bordella pertussis pertussis toxin subunit 1 100ng. Secondary. Goat polyclonal to rabbit IgG at 1/1000 dilution. Predicted band size: 36 kDa. Observed band size: 36 kDa.
Background:
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 α 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-α GTP-binding proteins from their membrane receptors.
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.
