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Chymotrypsin Protease (TLCK treated), MS Grade (Glyco-078CL)

Chymotrypsin Protease, MS Grade, is a purified native endoproteinase validated for maximum activity and selectivity in proteomic applications.      

Specifications
Product Size
4 x 25 µg
Final Product
Peptide
Workflow Step
Protein Digestion
Detection Method
Mass Spectrometry
Starting Material
Cell Lysate, Protein samples
For Use With (Equipment)
Mass Spectrometer
Contents & storage
Store at -20°C in a nonfrost-free freezer.
BACKGROUND
Description
This Chymotrypsin is a mass spectrometry (MS)-grade serine protease isolated from bovine pancreatic extracts. This chymotrypsin is TLCK-treated to eliminate tryptic activity. The selectivity of this enzyme is important for reproducible protein digestion and mass spectrometry-based protein identification. Chymotrypsin-digestion typically generates a larger number of shorter peptides compared to trypsin. This mass spectrometry-grade Chymotrypsin is packaged lyophilized (convenient 4 x 25 µg).
The endoproteinase chymotrypsin specifically cleaves at the carboxyl side of tyrosine, phenylalanine, tryptophan and leucine. Two predominant forms of chymotrypsin, A and B, are found in equal amounts in bovine pancreas. They are similar proteins (80% homology), but have different proteolytic characteristics. Both forms of chymotrypsin are present in Chymotrypsin. Since trypsin may co-purify with Chymotrypsin derived from natural sources, Chymotrypsin has been treated with TLCK to eliminate potential tryptic activity, improving digestion specificity. Chymotrypsin can tolerate mild denaturing conditions, such as 0.1% SDS, 2M urea, 2M guanidine·HCl, 1% CHAPS, and 30% acetonitrile with optimal activity in the pH range 7.5 to 8.5. This lyophilized enzyme has a mass of 25 kDa and is stable for 1 year when stored at -20°C.

For lab research use only, not for diagnostic, therapeutic or any in vivo human use.

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