Mass Spectrometry, sequencing grade and general proteases.
Name (A - Z)
Name (Z - A)
Ficin (or Ficain) is a cysteine protease enzyme (EC 220.127.116.11) 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 18.104.22.168) 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..
G-Biosciences Immobilized Soybean Trypsin Inhibitor (STI) resin is designed for the efficient removal of trypsin, chymotrypsin and elastase proteases from protein digests. The action of th..
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..
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 desi..
Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachium alkaline phosphatase) (EC 22.214.171.124) 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..
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 arginy..