Pertussis Toxin (islet-activating protein), a toxin originally isolated from Bordetella pertussis, has been shown to catalyze ADP-ribosylation of a protein in membrane preparation from rat C6 glioma cells. In addition, exposure of Chinese hamster ovary cells in culture to this compound has resulted in a clustered growth pattern response. Other experiments have shown Pertussis Toxin to block the ability of inhibitory hormones to reduce adenylate cyclase activity and enhance the ability of stimulatory hormones to activate the enzyme. Mechanistic studies have shown this toxin to consist of subunit A (active) promoter, which disrupts transmembrane signaling by ADP-ribosylating eukaryotic G-proteins, and B (binding) oligomer which helps the toxin bind to cells in vivo.

A toxin that blocks reduction of adenylate cyclase activity

>99%

Please note that this product is not activated. If your system requires activation, see Kaslow et al.,7 for suggested conditions.

CHO Cell Assay: When examined in a CHO cell assay as described by Hewlett et al.,5 the lowest concentration of toxin at which a positive response (clustered growth pattern) was obtained was 0.01 ng/ml.

Adenylate Cyclase Assay: The adenylate cyclase activity of this lot is 0.67 picomole/min/lJg in the presence of 1 μmolar calmodulin when assayed by the method of Wolff et al. 6

This product is provided as an aseptically packaged lyophilized powder, sealed under vacuum. Store at 4°C prior to and following reconstitution. DO NOT FREEZE.

Lyophilized solid

Soluble in water (Miscible). Reconstitute with sterile purified water or the sterile buffer of your choice. The resulting suspension should be made uniform by gentle mixing prior to use. Do not sterile filter, as this will result in loss of material. For long term storage, reconstitute in a high ionic strength buffer, such as sterile 0.1 M sodium phosphate, pH 7.0, 0.5 M NaCI. Handle the product gently; do not vortex.

1. Bradford, M.M. (1976) Anal. Biochem. 72, 248-254.
2. Tamura, M., Nogomori, K., Murai, S., Yajima, M., Ito, K" Katada, T., Ui, M. and Ishi, S. (1982) Biochem. 21,5516-5522.
3. Wyckoff, M., Rodbard, O. And Chramback, A. (1977) Anal. Biochem.78, 459-482.
4. Laemmli, U.K. (1970) Nature 227, 680-685.
5. Hewlett, E.L., Sauer, K.T., Myers, G.A., Cowell, J.L. and Guerrant, R.L. (1983) Infect. Immun. 40, 1198-1203.
6. Wolff, J., Cook, G.H., Goldhammer, A.R. and Berkowitz, S.A. (1980) PNAS 77, 3841-3844.
7. Kaslow, H.R., Lim, L.-K., Moss, J. and Lesikar, D.O. (1987) Biochem. 26, 123-127.