ACHROMOPEPTIDASE Chemical Properties

storage temp. 

−20°C

form 

partially purified powder

color 

Colorless to light yellow

Safety Information

Hazard Codes 

Xn

Risk Statements 

42/43-42

Safety Statements 

36-45-22

WGK Germany 

3

MSDS

• Language:English Provider:SigmaAldrich

ACHROMOPEPTIDASE Usage And Synthesis

Description

Endoproteinase Lys-C, Sequencing Grade, can be used for specific cleavage of peptides.Endoproteinase Lys-C, Sequencing Grade, is a widely used serine protease, that specifically hydrolyzes amide, ester, and peptide bonds at the carboxylic side of lysin. Endoproteinase Lys-C is isolated from Lysobacter enzymogenes and is supplied as a lyophilizate.

Uses

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].

Application

Use Endoproteinase Lys-C, Sequencing Grade, for protein structure analysis and for sequence analysis. It is suitable to digest proteins in solution, in polyacrylamide gels or on blotting membranes.

References

[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. DOI:10.1021/pr060033z

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