Skip to Content
Merck
All Photos(2)

Documents

SAE0089

Sigma-Aldrich

Streptolysin O from Streptococcus pyogenes

≥1,000,000 units/mg protein, recombinant, lyophilized powder, expressed in E. coli

Synonym(s):

Streptolysin O from Streptococcus pyogenes, SLO

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
308-500-3
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77

Assay

≥95% (SDS-PAGE)

specific activity

≥1,000,000 units/mg protein

mol wt

60 kDa

UniProt accession no.

shipped in

ambient

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

General description

Streptolysin O (SLO) is an immunogenic, oxygen-labile toxin, hemolytic exotoxin which is reversibly activated by dithiothreitol. [1] It is released into the extracellular medium along with other toxins, including streptolysin S, during the growth of most strains of group A and many strains of groups C and G Streptococci. [1,2] SLO and Streptolysin S differ from each other in that SLO is immunogenic and oxygen-labile while Streptolysin S is oxygen-stable, nonimmunogenic and only active when associated with a carrier protein.[3] The hemolytic activity of SLO is mediated by formation of multimeric nanopores in cholesterol containing lipid membranes.

SLO may be used for cell permeabilization or hemolysis. The susceptibility of hemolysis by SLO varies significantly for erythrocytes from different animal species.[1] Permeabilization of cells using SLO has been performed on multiple cell types and for various applications. For instance it has been used to introduce antisense oligonucleotides into cultured eukaryotic cells;[3] to investigate the effect of guanine nucleotide analogues on phosphatidylinositol metabolism and protein kinase C (PKC) activation in live human T lymphocytes;[4] to monitor cholesterol oxidation within a membrane lipid bilayer; [5] and to label proteins inside living cells using external fluorophores.[6]

Application

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

Biochem/physiol Actions

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.
This product is produced by recombinant expression in Escherichia coli and contains the complete native protein sequence of SLO (Uniport ID: P0DF96 aa 34-571) without any added purification tags and has calculated molecular weight of 60,144 Dalton. The material is lyophilized from a solution containing 20 mM Sodium Hepes pH 7.5, 150 mM Sodium Chloride and 2 mM EDTA.

Unit Definition

Lyophilized powder containing Hepes buffer salts and EDTA.
One unit will cause 50% lysis of 50 ul of a 2% human red blood cell suspension in phosphate buffered saline, pH 7.4, at 37 °C for 30 minutes.

Pictograms

Skull and crossbones

Signal Word

Danger

Hazard Statements

Hazard Classifications

Acute Tox. 2 Dermal - Acute Tox. 2 Inhalation - Acute Tox. 2 Oral

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


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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

E L Barry et al.
BioTechniques, 15(6), 1016-1018 (1993-12-01)
Cellular uptake of antisense oligonucleotides is critical to their ability to inhibit gene expression. In the present study, phosphodiester oligodeoxynucleotides were introduced into cells during brief permeabilization with the pore-forming agent streptolysin O. The extent of antisense inhibition was dependent
Production, purification, and assay of streptolysin O.
J E Alouf et al.
Methods in enzymology, 165, 52-59 (1988-01-01)
J D Graves et al.
The Biochemical journal, 265(2), 407-413 (1990-01-15)
A method of membrane permeabilization of T lymphocytes with the bacterial cytotoxin streptolysin O has allowed the effect of guanine nucleotide analogues on phosphatidylinositol metabolism and protein kinase C (PKC) activation to be investigated. The data demonstrate that, in permeabilized
Atsushi Shoji et al.
Journal of pharmaceutical and biomedical analysis, 128, 455-461 (2016-07-01)
Streptolysin O (SLO), which recognizes sterols and forms nanopores in lipid membranes, is proposed as a sensing element for monitoring cholesterol oxidation in a lipid bilayer. The structural requirements of eight sterols for forming nanopores by SLO confirmed that a
Labeling Proteins Inside Living Cells Using External Fluorophores for Fluorescence Microscopy.
Kai Wen Teng et al.
eLife, 6 (2017-02-02)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service