Ficin (or Ficain) is a cysteine protease enzyme (EC 126.96.36.199) isolated from fig latex is that has the endopeptidase activity to cleave immunoglobulin G molecules in the hinge reason. Ficin is typ..
Papain is a cysteine protease enzyme (EC 188.8.131.52) that has the endopeptidase activity to cleave immunoglobulin G molecules in the hinge region. This cleavage results in the generation of three ..
Pepsin is a proteolytic enzyme that is routinely used for the generation of F(ab)2 fragments from immunoglobulin G (IgG). The pepsin has the ability to cleave the heavy chains near the hinge reg..
Immobilized Trypsin is TPCK Treated Trypsin immobilized on 4% agarose that eliminates the contamination of protein digests by the trypsin. The immobilized trypsin is readily removed by separatin..
Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachium alkaline phosphatase) (EC 184.108.40.206) is a non-specifc, broad spectrum serine protease that is isolated from the saprop..
SG-Arginine-C™ endopeptidase (Clostripain, from C. histolyticum) specifically hydrolyzes the carboxy peptide bond of Arginine. SG-Arginine-C™ has been modified chemically by a pr..
SG-Chymotrypsin™ is a serine endopeptidase, which predominantly cleaves peptide bonds on the carboxy side of tyrosine, phenylalanine and tryptophan. In addition, chymotrypsin has a low catalytic..
SG-Glutamic-C™ is a serine endopeptidase, from S. aureus V8, that is highly specific for the cleavage of peptide bonds at the carboxy side of either aspartic or glutamic acid, depending on the b..
SG-Lysine-C™ endopeptidase, from Lysobacter enzymogenes, is a serine protease highly specific in cleaving peptide bonds at the carboxy side of lysine. Highly purified preparations of SG-Lysine-C..
A Chemically Modified, TPCK treated, Affinity Purified Trypsin
Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, ar..