PROTEASE INHIBITOR COCKTAIL Struktur

PROTEASE INHIBITOR COCKTAIL

Bezeichnung:PROTEASE INHIBITOR COCKTAIL

CAS-Nr

Englisch Name:PROTEASE INHIBITOR COCKTAIL

CBNumberCB2314734

SummenformelNull

Molgewicht0

MOL-DateiMol file

PROTEASE INHIBITOR COCKTAIL physikalisch-chemischer Eigenschaften

Flammpunkt	85 °C
storage temp.	−20°C
Aggregatzustand	lyophilized powder
Wasserlöslichkeit	Fully miscible in water.

Sicherheit

Kennzeichnung gefährlicher	C,Xi
R-Sätze:	36/37/38-34-36/38
S-Sätze:	26-36/37/39-45-36-23-24
RIDADR	UN 3261 8/PG 2
WGK Germany	-

Gefahreninformationscode (GHS)

PROTEASE INHIBITOR COCKTAIL Chemische Eigenschaften,Einsatz,Produktion Methoden

R-Sätze Betriebsanweisung:
R36/37/38:Reizt die Augen, die Atmungsorgane und die Haut.
R34:Verursacht Verätzungen.
S-Sätze Betriebsanweisung:
S26:Bei Berührung mit den Augen sofort gründlich mit Wasser abspülen und Arzt konsultieren.
S36/37/39:Bei der Arbeit geeignete Schutzkleidung,Schutzhandschuhe und Schutzbrille/Gesichtsschutz tragen.
S45:Bei Unfall oder Unwohlsein sofort Arzt zuziehen (wenn möglich, dieses Etikett vorzeigen).
S36:DE: Bei der Arbeit geeignete Schutzkleidung tragen.
S23:Gas/Rauch/Dampf/Aerosol nicht einatmen(geeignete Bezeichnung(en) vom Hersteller anzugeben).
Verwenden
Phosphatase Inhibitor Cocktail is used to inhibitors with a broad specificity for serine, cysteine, and acid proteases, and aminopeptidases. It has been tested on a wide variety of cells and tissue extracts to isolate/maintain intact proteins without degradation.
Enzyminhibitor
Enzymatic proteolysis can be arrested or minimized through the use of socalled cocktails containing combinations of serine protease, cysteine protease, aspartic protease, and metalloprotease inhibitors. The following combinations (or cocktails) have proved to be highly effective in the isolation of intact proteins, and some have are so popular that they are commercially available. General Protease Cocktails typically contain AEBSF, E-64, bestatin, leupeptin, aprotinin, and sodium EDTA. The latter is included only if the protein or enzyme being purified does not require a divalent metal cofactor for structural integrity. Fungal and Yeast Protease Cocktails typically contain AEBSF, pepstatin A, E-64, and 1,10- phenanthroline. Mammalian Cell Protease Inhibitor Cocktails typically contain AEBSF, pepstatin A, E-64, bestatin, leupeptin, and aprotinin. (Other metal ion chelators, such as 0.5 mM EGTA, may be added to suppress the activity of calcium ion-dependent proteases such as calpain. Again, one must determine whether the protein or enzyme being purified does not require a divalent metal cofactor for structural intgrity or biological activity. Bacterial Extract Protease Cocktails typically contain AEBSF), pepstatin A, E-64, bestatin, and sodium EDTA. For convenience, the inhibitory properties of these reagents are summarized as follows. AEBSF: This broadspectrum serine protease inhibitor, which is stable in water for one month when stored at –20 °C, has an inhibitory range 0.1-1.0 mM. AEBSF also inhibits cysteine proteases, such as papain. Antipain: This inhibitor is effective against serine proteases (e.g., plasmin, thrombin and trypsin, but not chymotrypsin, as well as some cysteine proteases, such as calpain and papain. Its inhibitory range is 1-100 μM, with IC50 = 0.15 mg/mL for papain, 0.25 mg/mL for trypsin, 1.2 mg/mL for cathepsin A). Prepare at 10 mM in water. Aprotinin: This water-soluble inhibitor, which is stable for months, when stored at 4 °C, blocks and many serine proteases at 0.3 μM (or equimolar with proteinase), but is without effect on thrombin or bloodclotting factor Xa. Bestatin: This aminopeptidase inhibitor, which has an inhibitory range of 1-10 μM, is prepared as a 1 mM stock solution in methanol and stable for 1 month, when stored at –20 °C. Chymostatin: This chymotrypsin-like serine protease inhibitor blocks chymase and cathepsins A,B,D and G, as well as some cysteine proteases (including papain). Its inhibitory range is 10–100 μM; IC50 = 0.1 mg/mL for chymotrypsin). Stock solutions are prepared at 10 mM in DMSO. DFP: This highly effective broad-spectrum serine-protease inhibitor is also a highly toxic nerve poison, and a well-ventilated fume hood and heavy rubber gloves should be used to avoid inhalation or contact with skin. For safety, DFP should be prepared as a 200 mM solution in anhydrous isopropanol or propylene glycol and then diluted 60-100x into cell extract. In aqueous solution, DFP rapidly decomposes (t1/2 = 20 min in water). E-64: This thiol protease inhibitor, which is effective in the 1-10 μM concentration range, is prepared as a 1 mM stock solution in water and is stable 1-2 weeks at –20 °C. EDTA: This broad-spectrum metalloproteinase inhibitor (effective range = 1-10 mM) nonspecifically inhibits many metalloenzymes, especially those with metal ion Kd values above 1 mM. N-Ethylmaleimide: This chemical modifying agent inhibits most thiol-proteases by reacting irreversibly with essential active-site thiol groups. NEM is water-soluble at >10mg/ml, and must be prepared freshly. Leupeptin: This inhibitor blocks trypsin-like serine proteases, such as trypsin, chymotrypsin, chymase, pepsin and thrombin. Leupeptin inhibits selected cysteine proteases (calpain, cathepsin B, H & L and papain). The inhibitory range is 10-100 μM, with the following IC50 values: 2 mg/mL for trypsin; 8 mg/mL for plasmin; and 0.5 mg/mL for cathepsin B. When prepared at 10 mM in water, leupeptin is stable 6 months when s

PROTEASE INHIBITOR COCKTAIL Anbieter Lieferant Produzent Hersteller Vertrieb Händler.

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