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.
H9395
α-Hemolysin from Staphylococcus aureus
lyophilized powder, Protein ~60 % by Lowry, ≥10,000 units/mg protein
Synonyme(s) :
α-Toxin
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641,00 €
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1 150,00 €
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0.5 MG
641,00 €
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About This Item
Produits recommandés
Source biologique
Staphylococcus aureus
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥10,000 units/mg protein
Contient
sodium citrate buffer as balance
Composition
Protein, ~60% Lowry
Solubilité
H2O: soluble 0.49-0.51 mg/mL
Numéro d'accès UniProt
Température de stockage
2-8°C
Informations sur le gène
Staphylococcus aureus ... SAOUHSC_01121(3920722)
Description générale
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[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]
Actions biochimiques/physiologiques
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]
Conditionnement
Package size based on protein content
Définition de l'unité
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.
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 2
Organes cibles
Lungs,Blood
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
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
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
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
Luning Yu et al.
Biophysical journal, 120(9), 1537-1541 (2021-02-23)
The use of chaotropic reagents is common in biophysical characterization of biomolecules. When the study involves transmembrane protein channels, the stability of the protein channel and supporting bilayer membrane must be considered. In this letter, we show that planar bilayers
Contenu apparenté
Panorama des méthodes de lyse cellulaire et d'extraction protéique, comme la solubilisation par détergents, la lyse par congélation/décongélation, le choc osmotique, la sonication, la lyse cellulaire enzymatique et les techniques de fragmentation mécanique comme l'homogénéisation au Dounce, au Polytron ou au mortier et au pilon.
Cell lysis and protein extraction methods overview various techniques, from detergent solubilization to mechanical disruption, supporting research needs.
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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.
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