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Proteases and Protein-Cleaving Reagents

Purified and agarose-immobilized proteases for enzymatic proteolysis (cleavage or digestion) of proteins to facilitate amino acid sequencing, peptide analysis and polypeptide structural characterization.



Protease to cleave (release) terminal amino acids including proline from the C-terminus of peptides; immobilized form allows enzyme removal after treatment. 



Protease (serine endopeptidase for prothrombin); cleaves arginine in the sequence Ile-Glu-Gly-Arg; useful for His-tagged fusion protein engineering. 



Effectively cleave fusion tags from recombinant proteins with this protease that is dual-tagged for easy removal after cleavage. 



Sulfhydryl-specific protease (ficin) immobilized onto beaded agarose resin to enable controlled antibody fragmentation, especially of mouse IgG1. 



Cysteine-endopeptidase (papain) immobilized onto beaded agarose resin to enable generation and purification of Fab fragments from antibodies. 



Acidic endopeptidase (pepsin) immobilized onto beaded agarose resin to enable generation and purification of Fab and F(ab')2 fragments from antibodies. 



Protease to cleave at the carboxyl-side of aliphatic, aromatic or hydrophobic residues; digest-inactivate DNase and RNase in nucleic acid purification. 



Staphylococcus aureus V-8 protease and beaded resin with buffers to cleave only glutamic acid residues or both glutamic and aspartic acid sites. 



Endoprotease to cleave the carboxyl-side of Arg and Lys residues; TPCK-treated to block chymotrypsin activity; immobilized form allows enzyme removal after treatment. 


Instructions | MSDS | CofA
Product Instructions | MSDS | CofA  

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