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PTX S1 Protein, Bordetella pertussis, Recombinant (His)

Catalog No. TMPH-00207

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. PTX S1 Protein, Bordetella pertussis, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 28.2 kDa and the accession number is P04977.

PTX S1 Protein, Bordetella pertussis, Recombinant (His)

PTX S1 Protein, Bordetella pertussis, Recombinant (His)

Catalog No. TMPH-00207
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. PTX S1 Protein, Bordetella pertussis, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 28.2 kDa and the accession number is P04977.
Pack SizePriceAvailabilityQuantity
20 μg$39720 days
100 μg$76920 days
500 μg$1,78020 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
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. PTX S1 Protein, Bordetella pertussis, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 28.2 kDa and the accession number is P04977.
Species
Bordetella pertussis
Expression System
P. pastoris (Yeast)
TagN-6xHis
Accession NumberP04977
Synonyms
ptxA,Pertussis toxin subunit 1,NAD-dependent ADP-ribosyltransferase,Islet-activating protein S1
Amino Acid
DDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLDHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVIGACMARQAESSEAMAAWSERAGEAMVLVYYESIAYSF
Construction
35-269 aa
Protein Purity
> 90% as determined by SDS-PAGE.
Molecular Weight28.2 kDa (predicted)
FormulationTris-based buffer, 50% glycerol
Reconstitution
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research 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 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.

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