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Merck

H9395

α-Hemolysin from Staphylococcus aureus

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

Synonym(s):

α-Toxin

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.56
MDL number:

Product Name

α-Hemolysin from Staphylococcus aureus, lyophilized powder, Protein ~60 % by Lowry, ≥10,000 units/mg protein

biological source

Staphylococcus aureus

form

lyophilized powder

specific activity

≥10,000 units/mg protein

contains

sodium citrate buffer as balance

composition

Protein, ~60% Lowry

solubility

H2O: soluble 0.49-0.51 mg/mL

UniProt accession no.

storage temp.

2-8°C

Quality Level

Gene Information

Staphylococcus aureus ... SAOUHSC_01121(3920722)

Packaging

Package size based on protein content

Application

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.

Biochem/physiol Actions

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.

General description

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.

Other Notes

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.

pictograms

Health hazardExclamation mark

signalword

Warning

Hazard Classifications

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

target_organs

Lungs,Blood

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
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.
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
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
Generation of chip based microelectrochemical cell arrays for long-term and high-resolution recording of ionic currents through ion channel proteins
Zheng T, et al.
Sensors and Actuators B, Chemical, 205 (205)

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