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ChemicalBook--->CAS DataBase List--->72561-05-8

72561-05-8

72561-05-8 Structure

72561-05-8 Structure
IdentificationBack Directory
[Name]

ENDOPROTEINASE LYS-C
[CAS]

72561-05-8
[Synonyms]

PROTEASE
EC 3.4.21.50
ENDOPROTEINASE LYS-C
ENDOPROTEINASE LYS-C USP/EP/BP
Proteinase, Myxobacter AL-1, II
Endoproteinase Lys-C, ExcisionGrade
protease from lysobacter enzymogenes
Endoproteinase Lys-C, Sequencing Grade,
ENDOPROTEINASE LYS-C FROM LYSOB. ENZYMO
ENDOPROTEINASE LYS-C, LYSOBACTER ENZYMOGENES
Recombinant Lysyl Endopeptidase (with His Tag)
Endoproteinase Lys-C from Lysobacter enzymogenes
Native Lysobacter enzymogenes Endoproteinase Lys-C
endoproteinase lys-C from lysob. enzymog enes 3U/vial (0.1mg
Endoproteinase Lys-C, Sequencing Grade, Lysobacter enzymogenes
ENDOPROTEINASE LYS-C FROM LYSOBACTER ENZYMOGENES SEQUENCING GRADE
[EINECS(EC#)]

276-716-4
[MDL Number]

MFCD02253020
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[form ]

lyophilized powder
[color ]

White to off-white
[biological source]

bacterial (Lysobacter enzymogenes)
[Water Solubility ]

water: soluble
[Specific Activity]

≥200units/mg protein ( at 25 °C, with Chromozym PL)
Safety DataBack Directory
[Symbol(GHS) ]


GHS07,GHS08
[Signal word ]

Danger
[Hazard statements ]

H315-H317-H319-H334-H335
[Precautionary statements ]

P261-P280-P305+P351+P338-P342+P311
[Hazard Codes ]

Xn
[Risk Statements ]

36/37/38-42/43
[Safety Statements ]

22-26-36/37-45
[WGK Germany ]

3
[F ]

3-10-21
Hazard InformationBack Directory
[Uses]

Endoproteinase Lys-C from Lysobacter enzymogenes is useful in the determination of primary structures of proteins. It has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody.
[General Description]

Endoproteinase Lys-C is an enzyme that preferentially cleaves at the carboxyl side of lysine residues.
[Biochem/physiol Actions]

Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36.
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