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Merck
CN

P2289

Endoproteinase Lys-C from Lysobacter enzymogenes

lyophilized powder

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About This Item

CAS Number:
UNSPSC Code:
12352204
EC Number:
276-716-4
MDL number:
EC Number:
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form

lyophilized powder

Quality Segment

analyte chemical class(es)

amino acids

packaging

vial of ≥3.0 units

storage temp.

2-8°C

General description

Endoproteinase Lys-C is an enzyme that preferentially cleaves at the carboxyl side of lysine residues.

Application

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.
Endoproteinase Lys-C has been used for the digestion monoclonal antibodies for disulfide bond assignment.

Biochem/physiol Actions

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

Other Notes

One unit will hydrolyze 1.0 μmole of N-p-tosyl-Gly-Pro-Lys p-nitroanilide per min at pH 7.7 at 25 °C.


pictograms

Health hazardExclamation mark

signalword

Danger

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

wgk

WGK 1

Regulatory Information

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Hiromi Ito et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 806(1), 11-17 (2004-05-20)
Formation of covalently bound protein adducts with 2-arylpropionic acids (2-APAs) has been proposed as a possible explanation for hypersensitivity and toxic responses to chiral carboxylic acid drugs. To identify the cellular proteins chemically modified with optically active (S)-ibuprofen, we generate
Wei Zhang et al.
Analytical biochemistry, 311(1), 1-9 (2002-11-21)
Recombinant monoclonal antibodies (mAbs) are an emerging therapeutic area. However, there are few reports on disulfide bond assignment of recombinant mAbs. This work describes the complete disulfide bond assignment of a recombinant immunoglobulin G4 (IgG4) mAb. N-ethylmaleimide (NEM) was used
The effects of substrates, products and other ligands on the susceptibility ofinositol monophosphatase to proteolysis by endoprotease lys-C.
Gee NS
FEBS Journal, 284, 95-97 (1991)