Enzymes & Inhibitors

2 component microwell phosphatase substrate with excellent performance characteristics and a wide working range. Develops blue reaction product measurable at 490, 550, or 620 nm.

ApopTag&reg Peroxidase in situ detection kits label apoptotic cells in research samples by modifying DNA fragments utilizing terminal deoxynucleotidyl transferase (TdT) for detection of apoptotic cells by immuno-peroxidase detection of

ApopTag&reg Peroxidase in situ detection kits label apoptotic cells in research samples by modifying DNA fragments utilizing terminal deoxynucleotidyl transferase (TdT) for detection of apoptotic cells by immuno-peroxidase detection of

Apoptosis Activator VII, Apoptozole CAS 1054543-47-3 Calbioc

Ready-to-use high quality apoptosis inducers allow users an easy tool for induction of apoptosis in cultured cells. These stabilized reagent solutions have a long storage life and are easy to use.

Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein, and plasmin. Material is provided as a solution containing 10,000 KIU/mL of aprotinin.

Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein, and plasmin. Material is provided as a solution containing 10,000 KIU/mL of aprotinin.

Also known as bovine pancreatic trypsin inhibitor. Activity: Approx 6,000 KIU/mg Specificity: A broad range, competitive and reversible inhibitor of chymotrypsin, plasmin, trypsin, kallikrein and other serine proteases Solubility: Soluble in water

Competitive serine protease inhibitor which forms stable complexes with and blocks the active sites of enzymes. The binding is reversible, and most aprotinin-protease complexes dissociate at a pH&gt10 or &lt3.

Competitive serine protease inhibitor which forms stable complexes with and blocks the active sites of enzymes. The binding is reversible, and most aprotinin-protease complexes dissociate at a pH&gt10 or &lt3.

Competitive serine protease inhibitor which forms stable complexes with and blocks the active sites of enzymes. The binding is reversible, and most aprotinin-protease complexes dissociate at a pH&gt10 or &lt3.

Competitive serine protease inhibitor which forms stable complexes with and blocks the active sites of enzymes. The binding is reversible, and most aprotinin-protease complexes dissociate at a pH&gt10 or &lt3.