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Enzymes accelerate, or catalyze, chemical reactions, and they are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Choose specific enzymes for cleaving bonds, removing genomic DNA from RNA preparations, for producing fragments of proteins, or for use in ion exchange chromatography. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required.
Description:
Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues and typically there is little or no cleavage a
Description:
G-Biosciences' mass spectrometry grade trypsin is a chemically methylated to yield an enzymatically active protein with maximum trypsin specificity and is extremely resistant to autolysis.
Description:
Store lyophilized or in Resuspension Buffer (50mM acetic acid) at -20[degree]C. Sequencing Grade Modified Trypsin purified from porcine specifically hydrolyzes peptide bonds at the carboxylic sides of lysine and arginine residues.
Description:
Trypsin. Modified Mass Spec-Bovine, Highly Purified Mass Spectroscopy grade Trypsin. A serine endopeptidase, cleaves the carboxy side of arginine, lysine and s-aminoethyl cysteine, suitable for mass spectrometry and sequence analysis. 20ug/vial. Pack of 5 vials.
Description:
Arg-C (clostripain) is an endopeptidase that cleaves at the C-terminus of arginine residues, including the sites next to proline. Cleavage also will occur at lysine residues. Can be used alone or in combination with other proteases for protein analysis.
Description:
It is a serine protease that preferentially cleaves at the C-terminus of alanine, valine, serine, glycine, leucine or isoleucine. Elastase has a unique capability of digesting elastin. This enzyme can be used alone or in combination with other proteases for protein analysis.