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 typically used to cleave mouse IgG1 as this are difficult to cleave with papain and pepsin. In the..
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 ~50kDa fragments; two Fab domains and a Fc domain. The papain-digested antibody is unable to p..
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 region. One or more of the disulfide bonds that join the heavy chains in the hinge region are preserved..
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 separating the agarose from the digestion solution.
Trypsin is a serine endopeptidase that specific..
The InGel™ Blue kit provides a complete set of reagents for the in gel tryptic digestion and extraction of peptides for mass spectrometry (MALDI and LC MS/MS). The kit is specifically designed for use with Coomassie or fluorescent stained protein spots/bands.
The kit has all th..
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 saprophytic fungus Tritirachium album.
Proteinase K is routinely used for the purification ..
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 propriety process to render the enzyme resistant to autolysis and stabilize enzymatic activity. In addit..
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 activity against the carboxy side of leucine, methionine, alanine, aspartic and glutamic acids. It ..
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 buffer used. In Tris-HCl buffer, in particular in the absence of phosphate ions, the enzyme is specif..
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™ are chemically modified making the enzyme resistant to autolysis and stabilizing its enzymat..
Trypsin is a serine protease that cleaves peptides on C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7.0-8.0. Trypsin is inhibited by serine protease inhibitors including TLCK (N-p-tosyl-L-lysine chloromethyl ketone), PMSF (phenylmethanesulfonyl fluoride),..
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 crysta..