α-Toxin, Staphylococcus aureus

α-Toxin causes internucleosomal DNA degradation in T lymphocytes by forming small transmembrane pores. Many cell types are sensitive to cytolysis by α-toxin. Under certain conditions, nucleated cells can be treated with α-toxin without causing lysis. Under controlled conditions, α-toxin monomers bind to the cell membrane and form a hexamer, which functions as a hydrophilic pore with a 1-3 nm diameter. The cell becomes permeable to small molecules, while large molecules, such as enzymes or carbohydrates are excluded. The molecular weight cut-off of material passing through the pore is approximately 2-4 kDa. The pore is somewhat ion selective. Other agents commonly used for permeabilizing cells form large lesions in the membrane, making them permeable to macromolecules. α-Toxin has been utilized to introduce ions, substrates, inhibitors, nucleotides, and other pharmacological agents into cells, thereby regulating cell physiology or function. For example, the arachidonic acid cascade (and subsequent production of prostaglandin I₂) is triggered by α-toxin and PMNs in endothelial cells when pores are formed that allow the passive influx of Ca²⁺. Stimulates prostaglandin synthesis and enhances phosphorylation of myelin basic protein.

A monomer isolated from the Wood 46 strain of Staphylococcus aureus and purified by a modification of the methods of Harshman, et al., and Hohman. Stimulates prostaglandin synthesis and phosphorylation of myelin basic protein. Causes internucleosomal DNA degradation in T lymphocytes by forming small transmembrane pores.

Alpha Toxin, CAS 12616-52-3, is a major cytotoxin isolated and purified from the Wood 46 strain of Staphylococcus aureus. At low concentration it binds to cell surface receptors and forms heptameric pores.

Hemolytic activity: ≥30 units/µg.

Primary Target
Stimulates prostaglandin synthesis and phosphorylation of myelin basic protein.

Product does not compete with ATP.

Toxicity: Highly Toxic (H)

One unit is defined as the dilution of α-toxin that mediates 50% lysis of a 5% suspension of rabbit red cells.

Lyophilized from 10 mM sodium phosphate buffer, pH 7.2.

A single polypeptide chain protein isolated from the Wood 46 strain of Staphylococcus aureus and purified by a modification of the methods of Harshman, S., et al. (1988) and Hohman R.J. (1988).

Following reconstitution, refrigerate (4°C). Stock solutions are stable for one week at 4°C.

Reconstitute with 500 μL of sterile distilled H2O

Single band by SDS-PAGE

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Jonas, D., et al. 1994. Infect. Immun.62, 1304.
Cescatti, L., et al. 1991. J. Membr. Biol.119, 53.
Harshman. S., et al. 1988. Methods Enzymol.165, 3.
Hohman, R.J. 1988. Proc. Natl. Acad. Sci. USA 85, 1624.

Not available for sale outside of the United States.

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