Streptolysin O from Streptococcus pyogenes

Permeabilizes membranes to permit cellular uptake of large or charged molecules.

Streptolysin O is a toxin secreted by Streptococcus pyogenes and is a prototype member of poreforming bacterial cytolysins. It is used permeabilize cell membranes to permit cellular uptake of large or charged molecules. It is used to study macromolecule delivery. It is a potential anticancer agent and is used to study suicide cancer gene therapy.

Used to create holes (reversible pores) in cholesterol-enriched plasma membranes of eukaryotic cells allowing selective permeabilization with molecules such as proteins (up to 100 kDa) and siRNAs.

Streptolysin O possesses a single polypeptide chain with a molecular weight of f62 kDa. Streptolysin O binds to membrane cholesterol and oligomerizes to create a ring structure that consists of 45 to 50 units. The ring structure inserts into the membrane to make a large pore (25 to 30 nm), which DNA, RNA, peptides and proteins may pass. It is thiol-activated. It is inhibited by allicin, an active component of garlic.

Thiol-activated toxin that permeabilizes animal cell membranes. The protein binds as a monomer to membrane cholesterol and subsequently polymerizes into large arc- and ring-shaped structures surrounding pores of >12 nm.

Thiol-activated toxin that permeabilizes animal cell membranes..

25KU

Lyophilized powder containing Tris buffer salts, sodium azide, PMSF, and EDTA.

Keep container tightly closed in a dry and well-ventilated place. Keep in a dry place

One unit will cause 50% lysis of 2% red blood cell suspensions in phosphate buffered saline, pH 7.4, after incubation at 37 °C for 30 min.