| Identification | Back Directory | [Name]
ACHROMOPEPTIDASE | [CAS]
123175-82-6 | [Synonyms]
PEPTIDASE TBL-1
ACHROMOPEPTIDASE
Endoprotease LysC
Endo-Lys-C protease
Endopeptidase Lys-C
LYSYL ENDOPEPTIDASE
ACHROMOPEPTIDASE(R)
LYSYL ENDOPEPTIDASE(R)
achromopeptidase crude
Achromobacter protease I
Achromobacter proteinase I
Lysine-specific proteinase
Lysyl Endopeptidase Solution
ACHROMOPEPTIDASE, EC 3.4.21.50
Native Bacteria Achromopeptidase
achromopeptidase partially purified
Recombinant Lysyl Endopeptidase (Lys-C)
achromopeptidase from achromobacter lyticus
Native Achromobacter lyticus Achromopeptidase | [MDL Number]
MFCD00130333 |
| Hazard Information | Back Directory | [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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