Protease inhibitor cocktails are a unique series of enzyme inhibitors that knock out specific proteases to avoid peptide bond hydrolysis and subsequent protein destruction. Protease inhibitors are vital to scientists engaged in proteomic research, protein expression, characterization, protein modification, protein profiling, and quantitative measurement of proteins to prevent destructive protein degradation.
Properties of specific Protease, Phosphatase, Serine Protease Inhibitors Protease inhibitor cocktails are a unique series of enzyme inhibitors that knock out specific proteases to avoid peptide bond hydrolysis and subsequent protein destruction. Protease inhibitors are vital to scientists engaged in proteomic research, protein expression, characterization, protein modification, protein profiling, and quantitative measurement of proteins to prevent destructive protein degradation.[Get your Free Inhibitor Brochures here]
Phosphatases play an important role in many signal transduction pathways, as the addition or removal of a phosphate group can activate or de-activate an enzyme, or allow a particular protein-protein interaction. Phosphatase inhibitors vary in function, targeting specific unwanted phosphatases to prevent their activity. Combinations of inhibitors in cocktail form can selectively target particular contaminants. A.G. Scientific maintains a selection of standard inhibitor cocktails in stock, and retains the ability to prepare custom formulations.| Inhibitor | Target for Inhibition | Specifics |
| AEBSF | Serine proteases such as thrombin, plasmin, kallikrein, chymotrypsin, and trypsin | Irreversible inhibitor, lower toxicity than PMSF or DFP. |
| Leupeptin | Serine and cysteine proteases. Often used for inhibition of plasmin, trypsin, papain, kallikrein, and cathepsin B. | Reversible inhibitor |
| Antipain | Papain and trypsin, and to a smaller extent plasmin | More specific to papain and trypsin than leupeptin and 100-fold more potent than elastatinal. |
| Aprotinin | Kallikrein, trypsin, chymotrypsin, and various serie proteases | Competitive, reversible inhibitor |
| E-64 | Cysteine proteases | Irreversible inhibitor |
| Pepstatin A | Aspartic proteases. Pepsin, cathespin D, rennin, chymosin, and HIV proteases. | Reversible inhibitor |
| Bestatin | Aminopeptidase | Binds to cell surfaces. Also activates macrophages and T lymphocytes. |
| Phosphoramidon | Endothelin converting enzyme IC50 = 0.68μM | Also inhibits neutral endopeptidase 24.11 and neprilysin 2 |
| Calyculin A | Protein phosphatase 1 and 2A | Also potent non-phorbol tumor promoter |
| Microcystin LR | Protein phosphatase 1 and 2A | Potent inhibitor |
| Cantharidin | Protein phosphatase 2A | Also inhibits protein phosphatase 1 at higher concentrations. Useful in inhibition of PP-1 and PP-2A during purification of phosphorylated proteins. |
| Bromotetramisole | Alkaline phosphatases | |
| Elastinal | Elastase-like serine proteases produced by actinomycetes | Competitive inhibitor. Also inhibits PMSF-stimulated degredation of histone H1 and HMG proteins and α2-macroglobulin-protease complexes. |
| GGACK (click for your free GGack Brochure) | Urokinase (IC50 < 1 μM) and Factor Xa | Irreversible inhibitor |