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
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biological source
Staphylococcus aureus
Quality Level
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
Gene Information
Staphylococcus aureus ... SAOUHSC_01121(3920722)
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.
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.
Packaging
Package size based on protein content
Unit Definition
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.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 2
Target Organs
Lungs,Blood
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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.
Bryan J Berube et al.
Toxins, 5(6), 1140-1166 (2013-07-31)
Staphylococcus aureus secretes a number of host-injurious toxins, among the most prominent of which is the small β-barrel pore-forming toxin α-hemolysin. Initially named based on its properties as a red blood cell lytic toxin, early studies suggested a far greater
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