Ficin (or Ficain) is a cysteine protease enzyme (EC 184.108.40.206) isolated from fig latex is that has the endopeptidase activity to cleave immunoglobulin G molecules in the hinge reason. Ficin is ty..
Papain is a cysteine protease enzyme (EC 220.127.116.11) 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 18.104.22.168) 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 prop..
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 ..
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™ ar..
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, arginine and l..