Chemical agents used to modify the amino acid side chains of proteins in order to alter their native charges, block or expose reactive binding sites, inactivate functional groups, and change functional groups to create targets for crosslinking and labeling.
Cleave the carboxyl-side of Arg and Lys residues with trypsin that isTPCK-treated to block chymotrypsin activity; its immobilized form allows enzyme removal after digestion.
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Enable controlled antibody fragmentation, especially of mouse IgG1, with this sulfhydryl-specific ficin protease immobilized onto beaded agarose resin.
Efficiently reduce protein or peptide disulfide bonds with this stable, odorless, beaded agarose resin on which Tris (2-carboxyethyl) phosphine is immobilized.
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Specifically cleave only at glutamic acid residues or cleave at both glutamic and aspartic residues with our immobilized Staphylococcus aureus V-8 protease kit.