Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues. Typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. This trypsin is purified from bovine pancreas, 1X…

Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachiumalkaline phosphatase) (EC 3.4.21.64) is a non-specifc, broad spectrum serine protease that is isolated from the saprophytic fungus Tritirachium album. Proteinase K is routinely used for the purification of target…

4-(2-Aminoethyl) benzenesulfonyl fluoride hydrochloride Specificity: Specific irreversible inhibitor of serine proteases, including chymotrypsin, kallikrein, plasmin, thrombin and trypsin. A stable non-toxic alternative to PMSF. Solubility: Soluble in water Features …