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Streptolysin O (≥1000000 units/mg) Sale

(Synonyms: 链球菌溶血素 O) 目录号 : GC65447

Streptolysin O (≥1000000 units/mg) 是一种 A 组链球菌毒素,是一种经过充分表征的胆固醇结合细菌外毒素的氧不稳定原型。

Streptolysin O (≥1000000 units/mg) Chemical Structure

Cas No.:98072-47-0

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25KU
¥7,650.00
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产品描述

Streptolysin O (≥1000000 units/mg) is a ≥1000000 units/mg Streptolysin O . Streptolysin O, a group A streptococcal toxin, is a well-characterized oxygen-labile prototype of a cholesterol-binding bacterial exotoxin. Streptolysin O causes both lysis of cells and cardiotoxicity. Streptolysin O is widely used for the controlled permeabilization of cell membranes. Streptolysin O exists in two forms, a reduced active state and an oxidized reversibly inactive state[1][2][3][4].

[1]. Sierig G, et al. Cytotoxic effects of streptolysin o and streptolysin s enhance the virulence of poorlyencapsulated group a streptococci. Infect Immun. 2003 Jan;71(1):446-55. [2]. Van Epps DE, et al. Streptolysin O II. Relationship of Sulfyhdryl Groups to Activity. Infect Immun. 1971 May;3(5):648-52. [3]. Uchiyama S, et al. Streptolysin O Rapidly Impairs Neutrophil Oxidative Burst and Antibacterial Responses to Group A Streptococcus. Front Immunol. 2015 Nov 16;6:581. [4]. Yamamoto I, et al. Mutational and comparative analysis of streptolysin O, an oxygen-labile streptococcal hemolysin. Biosci Biotechnol Biochem. 2001 Dec;65(12):2682-9.

Chemical Properties

Cas No. 98072-47-0 SDF Download SDF
别名 链球菌溶血素 O
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Research Update

Capacity of listeriolysin O, Streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells

Infect Immun 1992 Jul;60(7):2710-7.PMID:1612739DOI:10.1128/iai.60.7.2710-2717.1992.

The Listeria monocytogenes hemolysin listeriolysin O (LLO) plays a major role in mediating the escape of L. monocytogenes from a vacuolar compartment. In a previous report, it was shown that Bacillus subtilis expressing LLO could escape from a host vacuolar compartment and grow in the cytoplasm (J. Bielecki, P. Youngman, P. Connelly, and D. A. Portnoy, Nature [London] 345:175-176, 1990). In the present study, two related thiol-activated hemolysins, Streptolysin O (SLO) and perfringolysin O (PFO), were expressed in B. subtilis and their ability to mediate intracellular growth was monitored by visual inspection and by assaying for CFU. Like LLO, PFO was active within the vacuolar environment, whereas SLO showed negligible activity. However, expression of PFO seemed to damage the host cells. The pH of the vacuole probably had little to do with these results, since all three hemolysins showed full or enhanced activity at pH 5.5, although LLO showed greatly reduced activity at pH 7. In addition, neutralization of the pH within host vacuoles by using weak bases had little effect on the lysis of the vacuole. The lack of SLO activity is probably caused by its lower specific activity; the purified protein had 10-fold less activity on a molar basis. These results suggest that LLO is not unique in its capacity to mediate intracellular growth of B. subtilis.

Oxygen-stable hemolysins of group A streptococci. 8. Leukotoxic and antiphagocytic effects of streptolysins S and O

Infect Immun 1972 Oct;6(4):459-64.PMID:4634952DOI:10.1128/iai.6.4.459-464.1972.

Streptolysin S exists in a cell-bound form and as an extracellular complex between a nonspecific carrier (serum, serum albumin, ribonucleic acid [RNA], Triton, Tween) and a hemolytic moiety (probably a peptide) synthesized by streptococci. Although all the forms of streptolysin S, at 100 hemolytic units, killed mouse leukocyte monolayers, the time needed to kill 100% of the cells varied with the different streptolysin S preparations. Whereas 30 min was sufficient for the cell-bound hemolysin to kill all of the cells, 60 and 180 min were required when RNA streptolysin S and serum streptolysin S, respectively, were employed. Addition of 10% mouse serum to RNA streptolysin S or to cell-bound hemolysin delayed the killing of the leukocytes. The delayed killing observed with serum and albumin hemolysins is probably due to competition for the hemolytic moiety between the carrier molecules and target sites (phospholipids) upon the leukocyte membrane. Serum streptolysin S must be constantly incubated with the cells for 90 min for 100% of the cells to undergo cytopathic changes upon subsequent incubation for an additional 90 min. Streptolysin S inhibitor (trypan blue) added to the system after 30 or 60 min of incubation resulted in the killing of 50 and 100% of the leukocytes, respectively, when the cells were further incubated for 120 min. It is suggested that 30 min of incubation was not sufficient for the transfer of enough streptolysin S molecules upon the cell surface to allow killing of all of the cells. Sublethal amounts of streptolysin S, Streptolysin O, and saponin suppressed phagocytosis of streptococci by mouse peritoneal macrophages. This effect was abolished by inhibitors of streptolysin S (trypan blue) and of Streptolysin O and saponin (cholesterol). With sublethal amounts of streptolysin S, no inhibition of the reduction of nitro blue tetrazolium by nonphagocytosing cells was observed, but these amounts of streptolysin S caused a 50% inhibition of the reduction of nitro blue tetrazolium by phagocytosing leukocytes. It is suggested that some metabolic systems, which are normally enhanced during phagocytosis, have been affected by sublethal doses of streptolysin S. The results indicate that the in vivo production of small amounts of streptolysins S and O by group A streptococci may inhibit phagocytosis and may thus contribute to the invasiveness and pathogenicity of this microorganism.

Enzyme-linked immunosorbent assay for detection of Streptolysin O antibodies

J Clin Microbiol 1986 Jan;23(1):62-5.PMID:3700609DOI:10.1128/jcm.23.1.62-65.1986.

An enzyme-linked immumosorbent assay (ELISA), based upon the detection of Streptolysin O antibodies in human sera, was developed. Disposable polystyrene tubes, sensitized with Streptolysin O antigen, were used as the test vehicles. Corresponding antibodies, present in test sera, were detected by binding of the antibodies to goat anti-human immunoglobulin G conjugated to horseradish peroxidase. Demonstration of bound conjugate was accomplished by monitoring peroxidase activity spectrophotometrically at 450 nm, using 5-aminosalicylic acid as the indicator. A total of 97 human sera, previously analyzed by means of the anti-streptolysin O titration technique, were evaluated with the ELISA procedure. A direct quantitative relationship, found to be statistically significant, was demonstrated between Todd units and absorbance values obtained with ELISA.

Activation of human neutrophil metabolism by Streptolysin O

J Infect Dis 1980 May;141(5):680-5.PMID:7373090DOI:10.1093/infdis/141.5.680.

The effect of Streptolysin O on the metabolic activity of human neutrophils was examined. Streptolysin O, within the range of 3 to 75 hemolytic units, stimulated neutrophils to emit light. This chemiluminescence was the result of metabolic activation, as confirmed by oxygen uptake studies and the suppression of chemiluminescence by the metabolic inhibitor, 2-deoxyglucose. Free cholesterol, which prevents Streptolysin O from binding to membrane cholesterol, blocked the neutrophil chemiluminescent response to Streptolysin O. Extracellular calcium ions were necessary for the streptolysin O-stimulated chemiluminescent response of neutrophils. Some cell viability was lost, as measured by trypan blue uptake and neutrophil lysis within the range of Streptolysin O concentration that caused metabolic stimulation. These observations suggest a possible role for Streptolysin O as a pathogenic factor in streptococcal infections.

Growth of Streptococcus pyogenes and Streptolysin O production in complex and synthetic media

J Gen Microbiol 1983 Mar;129(3):643-51.PMID:6192200DOI:10.1099/00221287-129-3-643.

A comparative study of the growth of a highly haemolytic group A streptococcal strain in Trypticase-yeast extract medium and in a chemically defined medium was undertaken. Appreciable growth was obtained in the latter medium with the release of significant amounts (120 haemolytic units) of Streptolysin O. This indicates that toxinogenic factors present only in the peptones of complex media are not essential for biosynthesis and release of this cytolytic toxin, as is the case for many bacterial toxins. NADase was also released in the synthetic medium. Bacterial cell mass, growth rate, and Streptolysin O production were threefold higher in the complex medium. The effects of various carbohydrates on Streptolysin O production in complex medium are investigated. No repression of toxin formation by glucose was observed. The relationship between growth and toxinogenesis in streptococci and in other toxinogenic bacteria is discussed.