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616385
Sigma-Aldrichα-Toxin, Staphylococcus aureus - CAS 12616-52-3 - Calbiochem
Alpha Toxin, CAS 12616-52-3, is a major cytotoxin isolated and purified from the Wood 46 strain of Staphylococcus aureus. At low concentration it binds to cell surface receptors and forms heptameric pores.
More>>Alpha Toxin, CAS 12616-52-3, is a major cytotoxin isolated and purified from the Wood 46 strain of Staphylococcus aureus. At low concentration it binds to cell surface receptors and forms heptameric pores. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
A monomer isolated from the Wood 46 strain of Staphylococcus aureus and purified by a modification of the methods of Harshman, et al., and Hohman. Stimulates prostaglandin synthesis and phosphorylation of myelin basic protein. Causes internucleosomal DNA degradation in T lymphocytes by forming small transmembrane pores.<.p>
Hemolytic activity: ≥30 units/µg.
Catalogue Number
616385
Brand Family
Calbiochem®
References
References
Jonas, D., et al. 1994. Infect. Immun.62, 1304. Cescatti, L., et al. 1991. J. Membr. Biol.119, 53. Harshman. S., et al. 1988. Methods Enzymol.165, 3. Hohman, R.J. 1988. Proc. Natl. Acad. Sci. USA 85, 1624.
Product Information
CAS number
12616-52-3
Unit of Definition
One unit is defined as the dilution of α-toxin that mediates 50% lysis of a 5% suspension of rabbit red cells.
ATP Competitive
N
Declaration
Not available for sale outside of the United States.
Form
Solid
Formulation
Lyophilized from 10 mM sodium phosphate buffer, pH 7.2.
Stimulates prostaglandin synthesis and phosphorylation of myelin basic protein.
Purity
Single band by SDS-PAGE
Source
A single polypeptide chain protein isolated from the Wood 46 strain of Staphylococcus aureus and purified by a modification of the methods of Harshman, S., et al. (1988) and Hohman R.J. (1988).
Specific Activity
≥30 units/µg protein
Physicochemical Information
Cell permeable
N
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
RTECS
WI0195720
Safety Information
R Phrase
R: 26/27/28
Very toxic by inhalation, in contact with skin and if swallowed.
S Phrase
S: 36/37/39-45
Wear suitable protective clothing, gloves and eye/face protection. In case of accident or if you feel unwell, seek medical advice immediately (show the label where possible).
Product Usage Statements
Storage and Shipping Information
Ship Code
Ambient Temperature Only
Toxicity
Highly Toxic
Hazardous Materials Attention:
Due to the nature of the Hazardous Materials in this shipment, additional shipping charges may be applied to your order. Certain sizes may be exempt from the additional hazardous materials shipping charges. Please contact your local sales office for more information regarding these charges.
Storage
-20°C
Do not freeze
Ok to freeze
Special Instructions
Following reconstitution, refrigerate (4°C). Stock solutions are stable for one week at 4°C.
End use certificate
Y
Canadian export regulations
Due to the country and/or U.S. state of origin of the animal material used in this product, this product may not be exported to Canada.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Bestellnummer
GTIN
616385
0
Documentation
α-Toxin, Staphylococcus aureus - CAS 12616-52-3 - Calbiochem SDB
α-Toxin, Staphylococcus aureus - CAS 12616-52-3 - Calbiochem Analysenzertifikate
Titel
Chargennummer
616385
Literatur
Übersicht
Jonas, D., et al. 1994. Infect. Immun.62, 1304. Cescatti, L., et al. 1991. J. Membr. Biol.119, 53. Harshman. S., et al. 1988. Methods Enzymol.165, 3. Hohman, R.J. 1988. Proc. Natl. Acad. Sci. USA 85, 1624.
Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.
Revision
01-October-2007 RFH
Description
α-Toxin causes internucleosomal DNA degradation in T lymphocytes by forming small transmembrane pores. Many cell types are sensitive to cytolysis by α-toxin. Under certain conditions, nucleated cells can be treated with α-toxin without causing lysis. Under controlled conditions, α-toxin monomers bind to the cell membrane and form a hexamer, which functions as a hydrophilic pore with a 1-3 nm diameter. The cell becomes permeable to small molecules, while large molecules, such as enzymes or carbohydrates are excluded. The molecular weight cut-off of material passing through the pore is approximately 2-4 kDa. The pore is somewhat ion selective. Other agents commonly used for permeabilizing cells form large lesions in the membrane, making them permeable to macromolecules. α-Toxin has been utilized to introduce ions, substrates, inhibitors, nucleotides, and other pharmacological agents into cells, thereby regulating cell physiology or function. For example, the arachidonic acid cascade (and subsequent production of prostaglandin I2) is triggered by α-toxin and PMNs in endothelial cells when pores are formed that allow the passive influx of Ca2+. Stimulates prostaglandin synthesis and enhances phosphorylation of myelin basic protein.
Form
Solid
Formulation
Lyophilized from 10 mM sodium phosphate buffer, pH 7.2.
Source
A single polypeptide chain protein isolated from the Wood 46 strain of Staphylococcus aureus and purified by a modification of the methods of Harshman, S., et al. (1988) and Hohman R.J. (1988).
CAS number
12616-52-3
RTECS
WI0195720
Purity
Single band by SDS-PAGE
Specific activity
≥30 units/µg protein
Unit definition
One unit is defined as the dilution of α-toxin that mediates 50% lysis of a 5% suspension of rabbit red cells.
Solubility
Reconstitute with 500 µl of sterile distilled H₂O
Storage
-20°C
Do Not Freeze
Ok to freeze
Special Instructions
Following reconstitution, refrigerate (4°C). Stock solutions are stable for one week at 4°C.
Toxicity
Highly Toxic
References
Jonas, D., et al. 1994. Infect. Immun.62, 1304. Cescatti, L., et al. 1991. J. Membr. Biol.119, 53. Harshman. S., et al. 1988. Methods Enzymol.165, 3. Hohman, R.J. 1988. Proc. Natl. Acad. Sci. USA 85, 1624.