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Protein Cleavage Reagents

There are many methods used to identify the interaction sites between two or more proteins or protein subunits.
 
Proteolytic Mapping
A common method used is the use of proteolytic enzymes that cleave at specific protein regions.  Proteolytic mapping has several advantages, including the fact that reactions can be performed in-vitro under physiological conditions and only require a small amount of native protein.
Several proteases that are highly purified and chemically modified to prevent auotlysis are offered. The proteases offered are Glutamic-C, Lysine-C, Arginine-C, Chymotrypsin, Trypsin and Aspartic-N.
 
Chemical Mapping
In some cases, chemical reagents are used that cleave proteins at known sites.

  • BNPS-Skatole

    (2-(2'-Nitrophenylsulfonyl)-3-methyl-3-bromoindolenine)

      

  • MSG-Trypsin™

    Mass Spectrometry Grade Trypsin

      

  • SG-Arginine-C™

    Endopeptidase for the specific hydrolysis of the carboxy peptide bond of arginine

      

  • SG-Aspartic-N™

    Hydrolysis of peptide bonds on the N-terminus of aspartate & cysteine residues

      

  • SG-Chymotrypsin™

    Hydrolysis of peptide bonds on the carboxy side of tyrosine, phenylalanzine and tryptophan.....

      

  • SG-Glutamic-C™

    Cleaves peptide bonds at the carboxy side of either aspartic or glutamic acid

      

  • SG-Lysine-C™

    Cleaves peptide bonds at the carboxy side of lysine