Lysyl endopeptidase, Achromobacter sp  (Synonyms: Lys-C)

Lysyl endopeptidase, Achromobacter sp (Lys-C) catalyzes carboxyl oxygen exchange reaction. Lysyl endopeptidase has higher substrate binding affinities and higher catalytic rates at the acidic pHs than at the alkaline pHs^[1].

Product Information
Derived from Achromobacter, it is recombinantly expressed in Escherichia coli. This product is a serine protease that can highly specifically hydrolyze amides, esters, and peptide bonds on the carboxyl side of lysine. The optimal reaction pH is 9.0-9.5, and the optimal reaction temperature is 30-37°C. It can still maintain high enzyme activity in the presence of 4M urea or 0.1% SDS.
The storage solution is 20 mM Tris-HCl, pH 8.0.

Instructions
Protein digestion, the recommended digestion ratio is 1:50-1:200 (w/w, enzyme: protein), and digestion is carried out at 37°C overnight.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

123175-82-6

Liquid

Colorless to light yellow

[Lysyl endopeptidase, Achromobacter sp]

3.4.21.50

≥3.0 AU/mg soild

One activity unit is defined as the amount of enzyme that catalyze the formation of 1 μmol AC-LyspNA in 1 min at 37℃ in Tris-HCl buffer at 25 mmol/L, pH 9.0

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Hajkova D, et al. pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin. J Proteome Res. 2006 Jul;5(7):1667-73.  [Content Brief]