Saltar al contenido
Merck

H9395

Sigma-Aldrich

α-Hemolysin from Staphylococcus aureus

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

Sinónimos:

α-Toxin

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

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

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 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.

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
  • to test its osteogenesis suppressive effects in bone marrow stromal cells (BMSCs)
  • in the preparation of α-hemolysin molecular imprinted polymer (MIP) for Biacore and surface plasmon resonance

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.

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. It has a marked preference for rabbit red blood cells. α-hemolysin stimulates cellular phospholipases and induces a Ca2+ influx. It leads to membrane disruption of the endothelial barrier and leakage of cytoplasmic components and osmotic lysis of the cells. α-hemolysin is implicated in the pathogenesis of sepsis.

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)


Elija entre una de las versiones más recientes:

Certificados de análisis (COA)

Lot/Batch Number

¿No ve la versión correcta?

Si necesita una versión concreta, puede buscar un certificado específico por el número de lote.

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

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
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
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
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.
Rakez Kayed et al.
The Journal of biological chemistry, 284(7), 4230-4237 (2008-12-23)
Amyloid oligomers are believed to play causal roles in several types of amyloid-related neurodegenerative diseases. Several different types of amyloid oligomers have been reported that differ in morphology, size, or toxicity, raising the question of the pathological significance and structural

Contenido relacionado

An overview of cell lysis and protein extraction methods including detergent solubilization, freeze-thaw lysis, osmotic shock, sonication, enzymatic cell lysis, and mechanical disruption techniques such as Dounce, Polytron, and mortar and pestle homogenization.

An overview of cell lysis and protein extraction methods including detergent solubilization, freeze-thaw lysis, osmotic shock, sonication, enzymatic cell lysis, and mechanical disruption techniques such as Dounce, Polytron, and mortar and pestle homogenization.

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico