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S5265

Sigma-Aldrich

Streptolysin O from Streptococcus pyogenes

lyophilized powder, Protein ~3 % by Lowry, 25,000-50,000 U/vial

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About This Item

CAS Number:
98072-47-0
EC Number:
308-500-3
MDL number:
MFCD00132389
UNSPSC Code:
12352202
NACRES:
NA.85

form

lyophilized powder

Quality Level

200

specific activity

25,000-50,000 U/vial

mol wt

native 69 kDa

composition

Protein, ~3% Lowry

storage condition

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

color

white

solubility

H2O: soluble 1 mg/mL

antibiotic activity spectrum

neoplastics

Mode of action

cell membrane | interferes

storage temp.

2-8°C

Gene Information

Streptococcus pyogenes MGAS8232 ... slo(993428)

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Application

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

Biochem/physiol Actions

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.

Packaging

25KU

Unit Definition

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.

Physical form

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

Other Notes

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

Signal Word

Danger

Hazard Classifications

Acute Tox. 2 Dermal - Acute Tox. 2 Inhalation - Acute Tox. 2 Oral - Aquatic Chronic 2 - Eye Dam. 1 - Skin Irrit. 2

Storage Class Code

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Mohsen Arzanlou et al.
Journal of medical microbiology, 59(Pt 9), 1044-1049 (2010-06-12)
Streptolysin O (SLO) is a potent cytolytic toxin produced by almost all strains of group A streptococci and is considered an important virulence factor for this organism. In this study we investigated the effect of allicin and aqueous garlic extracts
Neurotransmitter interactions related to central dopamine neurons.
K G Lloyd
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Chen Chen et al.
Nanoscale, 10(11), 5154-5162 (2018-03-02)
Exosomes are small membrane vesicles secreted by a wide variety of cells. Studies have demonstrated that exosomal miRNAs can influence the biological processes of recipient cells. Therefore, direct imaging and tracking of exosomal miRNAs in living recipient cells are essential
Wan Seok Yang et al.
Molecular cancer therapeutics, 5(6), 1610-1619 (2006-07-05)
We cloned the streptolysin O gene from the Streptococcus pyogenes genome and tested the possibility of using it as an anticancer reagent. Transient transfection of the streptolysin O gene efficiently killed 293T cells after 12 hours of transfection as determined
John Popovich et al.
Frontiers in bioengineering and biotechnology, 8, 527-527 (2020-06-26)
Pore-forming and hemolytic toxins are bacterial cytotoxic proteins required for virulence in many pathogens, including staphylococci and streptococci, and are notably associated with clinical manifestations of disease. Inspired by adsorption properties of naturally occurring aluminosilicates, we engineered inexpensive, laboratory-synthesized, aluminosilicate
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