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Merck

H9395

Sigma-Aldrich

α-Hemolysin from Staphylococcus aureus

lyophilized powder, Protein ~60 % by Lowry, ≥10,000 units/mg protein

Sinónimos:

α-Toxin

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432,00 €
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About This Item

Número de CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.56

432,00 €


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origen biológico

Staphylococcus aureus

Nivel de calidad

Formulario

lyophilized powder

actividad específica

≥10,000 units/mg protein

contiene

sodium citrate buffer as balance

composición

Protein, ~60% Lowry

solubilidad

H2O: soluble 0.49-0.51 mg/mL

Nº de acceso UniProt

temp. de almacenamiento

2-8°C

Información sobre el gen

Staphylococcus aureus ... SAOUHSC_01121(3920722)

Descripción general

α-Hemolysin, a pore-forming cytotoxin[1] is an extracellular protein secreted by most strains of pathogenic Staphylococcus aureus. It is secreted as a water-soluble monomer and is a small β-barrel protein.[1]

Aplicación

α-Hemolysin from Staphylococcus aureus has been used:
  • as a component of electrolyte solution for testing pore formation in lipid bilayer using electrophysiological measurements[2]
  • to test its osteogenesis suppressive effects in bone marrow stromal cells (BMSCs)[3]
  • in the preparation of α-hemolysin molecular imprinted polymer (MIP) for Biacore and surface plasmon resonance[4]

α-Hemolysin was used in a study to test the efflux pump and haemolysin activity of Escherichia coli of dairy origin. It was also used to test its adaptation to benzalkonium chloride and the effect of ciprofloxacin on biofilm formation.[5]

Acciones bioquímicas o fisiológicas

α-Hemolysin is selectively hemolytic and the monomeric form binds to a membrane and specific receptors are not required for binding. Upon binding to biological membranes and/or artificial membranes, self-oligomerization occurs, resulting in ring structures (hexameric aggregates) believed to represent transmembrane pores, which are permeable to ions and small metabolites.[1] It has a marked preference for rabbit red blood cells.[6] α-hemolysin stimulates cellular phospholipases and induces a Ca2+ influx.[7] It leads to membrane disruption of the endothelial barrier and leakage of cytoplasmic components[1] and osmotic lysis of the cells.[6] α-hemolysin is implicated in the pathogenesis of sepsis.[4]

Envase

Package size based on protein content

Definición de unidad

One hemolytic unit will cause 50% lysis of a 1% suspension of rabbit red blood cells in phosphate buffered saline, pH 7.0, containing 1% bovine serum albumin after 30 min at 37 °C followed by refrigeration for 30 min at 4 °C.

Pictogramas

Health hazardExclamation mark

Palabra de señalización

Warning

Frases de peligro

Clasificaciones de peligro

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 2

Órganos de actuación

Lungs,Blood

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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Gregory J Digby et al.
The Journal of physiology, 586(14), 3325-3335 (2008-05-24)
Signalling by heterotrimeric G proteins is often isoform-specific, meaning certain effectors are regulated exclusively by one family of heterotrimers. For example, in excitable cells inwardly rectifying potassium (GIRK) channels are activated by G betagamma dimers derived specifically from G(i/o) heterotrimers.
Ankita Pagedar et al.
The Journal of dairy research, 79(4), 383-389 (2012-08-10)
The present study investigates the effect of adaptive resistance to ciprofloxacin (Cip) and benzalkonium chloride (BC) on biofilm formation potential (BFP), efflux pump activity (EPA) and haemolysin activity of Escherichia coli isolates of dairy origin. All the isolates, irrespective of
François Vandenesch et al.
Frontiers in cellular and infection microbiology, 2, 12-12 (2012-08-25)
One key aspect of the virulence of Staphylococcus aureus lies in its ability to target the host cell membrane with a large number of membrane-damaging toxins and peptides. In this review, we describe the hemolysins, the bi-component leukocidins (which include
D Fink et al.
Cellular signalling, 1(4), 387-393 (1989-01-01)
Staphylococcal alpha-toxin at subcytotoxic concentrations stimulated phosphatidylinositol turnover and arachidonic acid release in undifferentiated cultures of pheochromocytoma PC12 cells. Stimulation of phospholipase A2 but not C was dependent on extracellular calcium. Addition of staphylococcal alpha-toxin to PC12 cells caused a
Muhmmad Omar-Hmeadi et al.
Traffic (Copenhagen, Denmark), 19(6), 436-445 (2018-03-16)
Phosphoinositides (PtdIns) play important roles in exocytosis and are thought to regulate secretory granule docking by co-clustering with the SNARE protein syntaxin to form a docking receptor in the plasma membrane. Here we tested this idea by high-resolution total internal

Contenido relacionado

Cell lysis and protein extraction methods overview various techniques, from detergent solubilization to mechanical disruption, supporting research needs.

Los métodos de lisis celular y extracción de proteínas abarcan varias técnicas, desde la solubilización de detergentes hasta la ruptura mecánica, que respaldan las necesidades de investigación.

Preguntas

  1. We suspended in the product H9395 in 12.5 ml of PBS (our usual water-based infection solvent), flash-froze the aliquots in liquid nitrogen, and stored the aliquots at -80 C. There was no apparent issue with resuspension in PBS vs water. However, we observed no hemolytic activity in our in vivo mouse study or an in vitro quantitative hemolysis assay performed with rabbit blood.

    1 respuesta
    1. The stability of stock solutions of this enzyme has not been evaluated. However, it is cited in Methods in Enzymology, 165, 3-7 (1988) that at concentrations greater than 2 mg of protein per ml it can be stored at -20 °C without loss of hemolytic titer.

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