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P2289

Sigma-Aldrich

Endoproteinase Lys-C from Lysobacter enzymogenes

lyophilized powder

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About This Item

Numero CAS:
72561-05-8
Classificazione EC (Enzyme Commission):
3.4.21.50 (BRENDA, IUBMB)
Numero CE:
276-716-4
Numero MDL:
MFCD02253020
Codice UNSPSC:
12352204

Forma fisica

lyophilized powder

Livello qualitativo

200

Classi chimiche degli analiti

amino acids

Confezionamento

vial of ≥3.0 units

Temperatura di conservazione

2-8°C

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Descrizione generale

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

Applicazioni

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.

Azioni biochim/fisiol

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

Definizione di unità

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.

Pittogrammi

Health hazardExclamation mark
GHS08,GHS07

Avvertenze

Danger

Indicazioni di pericolo

H315,H317,H319,H334,H335

Classi di pericolo

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

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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

Certificati d'analisi (COA)

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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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