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P2289

Sigma-Aldrich

Endoproteinase Lys-C from Lysobacter enzymogenes

lyophilized powder

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About This Item

CAS Number:
72561-05-8
Enzyme Commission number:
3.4.21.50 (BRENDA, IUBMB)
EC Number:
276-716-4
MDL number:
MFCD02253020
UNSPSC Code:
12352204

form

lyophilized powder

Quality Level

200

analyte chemical class(es)

amino acids

packaging

vial of ≥3.0 units

storage temp.

2-8°C

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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.

Unit Definition

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
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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)
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
J G Jacobs et al.
Journal of virology, 85(23), 12537-12546 (2011-09-16)
Classical scrapie is a prion disease in sheep and goats. In sheep, susceptibility to disease is genetically influenced by single amino acid substitutions. Genetic breeding programs aimed at enrichment of arginine-171 (171R) prion protein (PrP), the so-called ARR allele, in
Pavlo Pristatsky et al.
Analytical chemistry, 81(15), 6148-6155 (2009-07-14)
The hinge region of human IgG2 contains four cysteine residues involved in disulfide linkages between the heavy chains, as well as the heavy and light chains. These linkages provide the fundamental framework of three distinct IgG2 disulfide isoforms recently described.
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