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SAE0089

Sigma-Aldrich

Streptolysine O from Streptococcus pyogenes

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

Synonyme(s) :

Streptolysin O from Streptococcus pyogenes, SLO

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
308-500-3
Numéro MDL:
Code UNSPSC :
12352202

Pureté

≥95% (SDS-PAGE)

Activité spécifique

≥1,000,000 units/mg protein

Poids mol.

60 kDa

Numéro d'accès UniProt

Conditions d'expédition

ambient

Température de stockage

2-8°C

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Description générale

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

Elle perméabilise les membranes, ce qui permet l′incorporation de molécules de grande taille ou chargées par les cellules.

Actions biochimiques/physiologiques

Toxine activée par les thiols qui perméabiliser les membranes de cellules animales. La protéine se lie sous forme de monomère au cholestérol membranaire et se polymérise ensuite, pour former des structures en grand arc de cercle et en anneau entourant des pores de > 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.

Définition de l'unité

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.

Pictogrammes

Skull and crossbones

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

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

Code de la classe de stockage

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

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Les clients ont également consulté

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)
Production, purification, and assay of streptolysin O.
J E Alouf et al.
Methods in enzymology, 165, 52-59 (1988-01-01)
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
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

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