Protein Cleavage Reagents

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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 and Trypsin.
Chemical Mapping
In some cases, chemical reagents are used that cleave proteins at known sites.
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  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, Mass Spectrometry Grade

A Chemically Modified, TPCK treated, Affinity Purified Trypsin Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and l..