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Pertussis toxin (Bordetella pertussis)

Ultra-pure pertussis toxin delivering optimal antigenicity
 
BML-G100-0050 50 µg 385.00 USD
Do you need bulk/larger quantities?
 
Replaces Prod. #: ALX-630-003

  • Higher specificity and sensitivity
  • Minimal lot-to-lot variation
  • Reproducible scale-up for bulk quantities
  • Lyophilized format for extended shelf-life

Product Specification

Alternative Name:Islet-activating protein, PTX, Holotoxin
 
Source:From Bordetella pertussis, strain 165.
 
CAS:70323-44-3
 
Formulation:Lyophilized. Containing sodium phosphate and sodium chloride.
 
Purity:≥99%
 
Purity Detail:This product migrates as five distinct bands when run on a 12% polyacrylamide SDS-urea gel. The five bands consist of one A protomer subunit (S1, MW=26.2 kDa) and four B oligomer subunits (S2, S3, 2x S4, S5; MW’s: 21.9, 21.9, 12.1, 10.9 kDa).
 
Shipping:Ambient
 
Long Term Storage:+4°C
 
Use/Stability:This preparation is lyophilized, aseptically packaged and sealed under vacuum. Do not vortex. Store at 4°C prior to and following reconstitution. Do not freeze. This toxin is considered to be biologically active. The lyophilized preparation will remain active for at least one year. After reconstitution with sterile water this product should remain active for at least six months if stored at 4°C. Each vial when reconstituted to 500 μl with sterile distilled water, contains 50.0 μg of pertussis toxin in 10 mM sodium phosphate buffer with 50 mM sodium chloride at pH 7.0. The toxin is insoluble and the resulting suspension should be made uniform by gentle mixing, not vortexing, prior to withdrawing aliquots. Do not sterile filter. For use with purified G proteins, the toxin must be structurally converted to artificially create a form of the toxin that interacts directly with G proteins. See Kaslow et al. (1987)

This product should be used only by technically qualified personnel. Good laboratory technique should be employed: Avoid mouth pipetting; wear gloves and other protective clothing; avoid inhalation; avoid contact with skin or open wounds; thoroughly wash any area of the body that comes in contact with the toxin with soap and water; wash eyes with water for fifteen minutes; exercise care when handling in hypodermic needles to avoid inadvertent intravenous or subcutaneous injection.
 
Handling:Aseptically packed, sealed under vacuum. Do not vortex. Do not freeze.
 
Scientific Background:Pertussis toxin consists of an enzymatically active A protomer subunit (S-1) which possesses both NAD+ glycohydrolase and ADP-ribosyltransferase activities and a B oligomer subunit (S-2, S-3, S-4, and S-5) which is responsible for attachment of the native toxin to eukaryotic cell surfaces. Pertussis toxin uncouples G proteins from receptors by ADP ribosylating a cysteine near the carboxy-terminus of the A subunit.
 

Product Literature References

Comprehensive analysis of chemokine-induced cAMP-inhibitory responses using a real-time luminescent biosensor: V. Felouzis, et al.; Cell. Signal. 28, 120 (2016), Application(s): Cell culture , Abstract;
In vivo immunomodulatory effects of adipose-derived mesenchymal stem cells conditioned medium in experimental autoimmune encephalomyelitis: F. Yousefi, et al.; Immunol. Lett. 172, 94 (2016), Application(s): Injection into mice, Abstract;
Metformin ameliorates the development of experimental autoimmune encephalomyelitis by regulating T helper 17 and regulatory T cells in mice: Y. Sun, et al.; J. Neuroimmunol. 292, 58 (2016), Application(s): Injected into mice, Abstract; Full Text
Treatment with NAD+ inhibited experimental autoimmune encephalomyelitis by activating AMPK/SIRT1 signaling pathway and modulating Th1/Th17 immune responses in mice: J. Wang, et al.; Int. Immunopharmacol. 39, 287 (2016), Application(s): Experimental autoimmune encephalomyelitis (EAE) induction, mice, Abstract;
GABAB receptors inhibit low-voltage activated and high-voltage activated Ca2+ channels in sensory neurons via distinct mechanisms: D. Huang, et al.; Biochem. Biophys. Res. Commun. 465, 188 (2015), Application(s): LVA and HVA channel inhibition , Abstract;
Protective effect of a novel Rho kinase inhibitor WAR-5 in experimental autoimmune encephalomyelitis by modulating inflammatory response and neurotrophic factors: Y.H. Li, et al.; Exp. Mol. Pathol. 99, 220 (2015), Application(s): Injection into mouse abdominal cavity, Abstract;
Amidate prodrugs of 9-[2-(phosphonomethoxy)ethyl]adenine as inhibitors of adenylate cyclase toxin from Bordetella pertussis: M. Šmídková, et al.; Antimicrob. Agents Chemother. 58, 664 (2014), Application(s): Cell Culture, Abstract; Full Text
Myelin Oligodendrocyte Glycoprotein (MOG35-55) Induced Experimental Autoimmune Encephalomyelitis (EAE) in C57BL/6 Mice: S. Bittner, et al.; J. Vis. Exp. 86, e51275 (2014), Application(s): Immunization, Abstract; Full Text
The therapeutic effects of MSc1 nanocomplex, synthesized by nanochelating technology, on experimental autoimmune encephalomyelitic C57/BL6 mice: S. Fakharzadeh, et al.; Int. J. Nanomedicine 9, 3841 (2014), Application(s): Immunization, Abstract; Full Text
Human apolipoprotein AI induces cyclooxygenase-2 expression and prostaglandin I-2 release in endothelial cells through ATP-binding cassette transporter A1: D. Liu, et al.; Am. J. Physiol. Cell Physiol. 301, C739 (2011), Application(s): Treatment of HUVEC, Abstract; Full Text
A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit: C. Locht & R. Antoine; Biochimie 77, 333 (1995), Abstract;
Pertussis toxin and target eukaryotic cells: binding, entry, and activation: H.R. Kaslow & D.L. Burns; FASEB J. 6, 2684 (1992), Abstract;
Structure-activity analysis of the activation of pertussis toxin: H.R. Kaslow et al.; Biochemistry 26, 123 (1987), Abstract;
Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin: E.L. Hewlett et al.; Infect. Immun. 40, 1198 (1983), Abstract;
Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model: M. Tamura et al.; Biochemistry 21, 5516 (1982), Abstract;

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