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P2289

Sigma-Aldrich

Endoproteinase Lys-C from Lysobacter enzymogenes

lyophilized powder

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About This Item

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204

forma

lyophilized powder

Nível de qualidade

classe(s) química(is) do analito

amino acids

embalagem

vial of ≥3.0 units

temperatura de armazenamento

2-8°C

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Descrição geral

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

Aplicação

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.

Ações bioquímicas/fisiológicas

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

Definição da unidade

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.

Pictogramas

Health hazardExclamation mark

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

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

Órgãos-alvo

Respiratory system

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

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


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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)
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
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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