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 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 prop..


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 ..


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™ ar..

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..