This broad-spectrum serine protease inhibitor (inhibitory range 0.1-1.0 mM) also inhibits cysteine proteases such as papain. (Stable in water for one month when stored at —20°C.) [Formula Name: 4-(2-aminoethyl)-benzene sulfonylfluoride].
Inhibits serine proteases (plasmin, thrombin and trypsin, but not chymotrypsin) as well as some cysteine proteases such as calpain and papain. (Inhibitory range = 1-100 mM;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. [Formula Name: (S)-carboxy-2-phenylethyl]carbamoyl-L-arginyl-L-valyl-L-arginal].
Effective against many serine proteases (0.3 mM or equimolar with proteinase), but without effect on thrombin or blood-clotting factor Xa (water-soluble and stable for months when stored at 4°C).
Inhibitor of aminopeptidases (inhibitory range = 1-10 mM). Prepare at 1 mM in methanol, stable for 1 month when stored at —20°C.
Inhibits chymotrypsin-like serine proteases (chymase cathepsins A,B,D and G) as well as some cysteine proteases, including papain (inhibitory range = 10-100 mM;IC50 = 0.1 mg/mL for chymotrypsin). Prepare at 10 mM in DMSO
[Formula Name: N-[((S)-carboxy-2-phenylethyl)carbamoyl]-a-[2-imidohexahydro-4(S)-pyrimidyl]-L-glycyl-L-leucyl-L-phenylalaninal].
Highly effective broad-spectrum serine-protease inhibitor. (Highly toxic nerve poison;prepare 200 mM in anhydrous isopropanol or propylene glycol;then dilute 60-100x into cell extract;rapidly decomposes (ti/2 = 20 min in water). Avoid inhalation or contact with skin.
[Formula Name: Di-isopropylfluorophosphate].
Inhibits most thiol-proteases (inhibitory range = 1-10 mM). Prepare at 1 mM in water;stable 1-2 weeks when stored at —20°C.
Broad-spectrum metalloproteinase inhibitor (inhibitory range = 1-10 mM). Caution: Nonspecifically inhibits many metalloenzymes, especially those with Kd values for metal ion that are above 1 mM.
[Formula Name: N,N,N',N'-Ethylenediamine tetraacetate].
Inhibits most thiol-proteases by reacting irreversibly with SH groups. Water-soluble at >10 mg/ml, must be prepared fresh.
Inhibits trypsin-like serine proteases such as trypsin, chymotrypsin, chymase, pepsin and thrombin. Inhibits selected cysteine proteases (calpain, cathepsin B, H and L and papain). (Inhibitory range = 10-100 mM; IC50 = 2 mg/mL for trypsin, 8 mg/mL for plamin, 0.5 mg/mL for cathepsin B.) Prepare at 10 mM in water, stable 6 months when stored at —20°C.
[Formula Name: N-propionyl-L-leucyl-L-leucyl-L-arginal].
Inhibits aspartic proteases such as renin, chymosin and pepsin (inhibits at 1 mM). Prepare at 1mM in methanol or DMSO.
Broad-spectrum metalloproteinase inhibitor (Inhibitory range = 1-10 mM). Prepare at 200 mM in methanol or DMSO. Caution: Nonspecifically inhibits many metalloenzymes, especially zinc- and manganese-dependent enzymes and those with Kd values for metal ion that are above 1 mM.
This broad-spectrum serine protease inhibitor (inhibitory range 0.1-1.0 mM) also inhibits cysteine proteases such as papain. Thiol proteinases are reactivated upon incubation with 1 mM 2-mercaptoethanol or dithiothreitol. (Soluble in DMSO for 1 month when stored at —20°C.) [Formula Name: Phenylmethylsulfonylchloride].
Potent metalloendoproteinase inhibitor, including thermolysin and elastases. Weak collagenase inhibitor; (inhibitory range = 1-10 mM). Prepare at 1 mM in water, stable for 1 month when stored at —20°C
Inhibits trypsin-like serine proteases (10-100 mM);must be freshly prepared at 10 mM in 1 mM HCl and then diluted 100x into cell extract.
[Formula Name: Tosyl-lysyl-chloromethylketone].
Inhibits chymotrypsin-like serine proteases (10-100 mM). Prepare at 10 mM in absolute ethanol, stable for one month at 4°C.
[Formula Name: Tosyl-phenylalanyl-chloromethylketone].
bacterial extracts: AEBSF, pepstatin A, trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane (E-64), bestatin, and sodium EDTA.
Finally, there is a pervasive, but mistaken presumption that the inclusion of protease inhibitors at a recommended level will completely block protein degradation. The problem is that some enzymes are exquisitely sensitive to proteolysis, and while many globular enzymes resist overall degradation, flexible loops and extended polypeptide chains may undergo proteolysis. One test of partial proteolysis is the use of MALDI-TOF mass spectroscopy to confirm the exact molecular mass of a purified enzyme or protein. A more convenient approach uses Universal Protease Substrate™ (Roche Applied Science) for rapid and high-sensitivity detection of trace protease activity or as a test of protease inhibitor effectiveness. Proteolysis of resorufin-labeled casein releases labeled peptides that can be measured spectrophotometrically or fluorimetrically. The concentration of liberated resorufin-labeled peptides is a direct assay of proteolytic activity (e.g., 0.1 mg pronase, trypsin, and endoproteinase Asp-N yield DAbs574nm values of 0.11, 0.07, and 0.09, respectively, in low-sensitivity 15-minute assays). The same firm offers a complete protease inhibitor cocktail in tablet form, using a proprietary blend of protease inhibitors formulated as a ready-to-use water-soluble tablet.
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