Description
Lysine endopeptidase (Lys-C) is a serine protease derived from Pseudomonas species, which recognizes lysine in proteins and can specifically hydrolyze amide, ester, and peptide bonds on the carboxyl side of lysine. This product is a recombinant lysine endopeptidase expressed by Escherichia coli, free from other miscellaneous proteases (such as Lys-N, Arg-C, and other serine proteases), and has the same specificity and activity as natural lysine endopeptidase.
Additionally, our company also provides recombinant trypsin (mass spectrometry grade) (Cat#20416ES), which cuts at the carboxyl end of lysine or arginine residues in proteins. Customers can choose according to their experimental needs.
Features
1.High activity，good stability.
2.High purity of recombinant protein, free from other miscellaneous proteases, and no animal origin.
Applications
1.Protein analysis, such as protein mass spectrometry, sequencing, and peptide mapping analysis.
2.Synthesis of lysine-related derivatives.
Specifications
|
Source |
E.Coli recombinant expression |
|
Purity |
＞95% |
|
Concentration |
1.0 mg/mL |
|
Specific activity |
≥3.0 AU/mg |
|
SDS-PAGE |
Single main band |
|
Molecular Weight |
29±3 kDa |
|
Storage Buffer |
5 mM NaAc，10 mM EDTA，pH=5.5 |
|
Unit Definition |
Under the condition of 25 mmol/L pH9.0 Tris-HCl buffer, at 37℃, the amount of enzyme required to catalyze the production of 1 μmol AC-Lys-pNA in 1 min is defined as one activity unit (AU) |
Storage
The product can be stored at -25 ~ -15℃ for one years.
Payment & Security
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FAQ
The product is for research purposes only and is not intended for therapeutic or diagnostic use in humans or animals. Products and content are protected by patents, trademarks, and copyrights owned by Yeasen Biotechnology. Trademark symbols indicate the country of origin, not necessarily registration in all regions.
Certain applications may require additional third-party intellectual property rights.
Yeasen is dedicated to ethical science, believing our research should address critical questions while ensuring safety and ethical standards.