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C8118

Sigma-Aldrich

Chymase human

recombinant, expressed in Pichia pastoris

Synonyme(s) :

Mast cell protease I

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About This Item

Numéro CAS:
97501-92-3
Numéro de classification (Commission des enzymes):
3.4.21.39 (BRENDA, IUBMB)
Numéro MDL:
MFCD00132173
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in Pichia pastoris

Niveau de qualité

300

Forme

liquid

Activité spécifique

≥40 units/mg protein

Poids mol.

~37 kDa by SDS-PAGE

Concentration

125-400 μg/mL

Numéro d'accès UniProt

P23946

Application(s)

diagnostic assay manufacturing

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

human ... CMA1(1215)

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Catégories apparentées

Application

Human chymase has been used in a study to assess the effects of Panax notoginseng flower extract on the TGF-β/Smad signal transduction pathway in heart remodeling. Human chymase has also been used in a study to investigate the blood glucose level and survival in streptozotocin-treated human chymase transgenic mice.
Chymase has been implicated in generation of angiotensin II and cleavage of big endothelin. Studies indicate it may be involved in vascular proliferation, myocardial infarction and dermatitis.

Actions biochimiques/physiologiques

The enzyme rapidly converts angiotensin I to angiotensin II. Optimum pH for the enzyme activity is between 7.5 and 9.0. Enzyme activity is inhibited by soybean trypsin inhibitor, phenylmethylsulfonyl fluoride and chymostatin.

Propriétés physiques

Chymase is a cathepsin G-like, S1 serine proteinase found primarily in mast cells. It has a molecular mass of ~30 kDa, however its apparent molecular mass on SDS-PAGE is around 37 kDa.

Définition de l'unité

One unit hydrolyzes one micromole of N-benzoyl-L-tyrosine ethyl ester (BTEE) per minute at pH 7.8 and 25 °C. The assay buffer used to determine the enzyme activity contains 27 mM Tris-HCl, pH 7.8, with 150 mM NaCl and 0.43 mM BTEE.

Forme physique

Supplied as a solution in 20 mM Tris, 0.8 M NaCl and 25% glycerol, pH 7.6

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000090049
088M4167V
11180822
11150513
115M4086V

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Consulter la Bibliothèque de documents

Laurent L Reber et al.
Journal of immunology (Baltimore, Md. : 1950), 192(4), 1847-1854 (2014-01-24)
Mast cells (MCs) are found in large numbers in lungs of patients with pulmonary fibrosis. However, the functions of MCs in lung fibrosis remain largely unknown. We assessed the role of MCs and MC protease 4 (MCPT4), the mouse counterpart
Lora G Bankova et al.
Journal of immunology (Baltimore, Md. : 1950), 192(6), 2812-2820 (2014-02-14)
We previously established a mast cell (MC)-dependent thermal injury model in mice with ulceration and scar formation that depended on nonredundant functions of mouse MC protease (mMCP)4 and mMCP5. We hypothesized that MC activation is an early event and now
J C Powers et al.
Biochemistry, 24(8), 2048-2058 (1985-04-09)
The extended substrate binding sites of several chymotrypsin-like serine proteases, including rat mast cell proteases I and II (RMCP I and II, respectively) and human and dog skin chymases, have been investigated by using peptide 4-nitroanilide substrates. In general, these
I Waern et al.
Mucosal immunology, 6(5), 911-920 (2012-12-14)
Mast cells (MCs) are major effector cells contributing to allergic conditions. When activated, they can release large amounts of active proteases, including chymase from their secretory granules. Here we assessed the role of the chymase mouse mast cell protease 4
Thomas Lind et al.
Matrix biology : journal of the International Society for Matrix Biology, 112, 1-19 (2022-08-01)
Mast cells have been linked to osteoporosis and bone fractures, and in a previous study we found that mice lacking a major mast cell protease, chymase, develop increased diaphyseal bone mass. These findings introduce the possibility that mast cell chymase
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