C8118
Chymase human
recombinant, expressed in Pichia pastoris
Sinónimos:
Mast cell protease I
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
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Permítanos ayudarleNombre del producto
Chymase human, recombinant, expressed in Pichia pastoris
recombinant
expressed in Pichia pastoris
form
liquid
specific activity
≥40 units/mg protein
mol wt
~37 kDa by SDS-PAGE
concentration
125-400 μg/mL
UniProt accession no.
application(s)
diagnostic assay manufacturing
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CMA1(1215)
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Categorías relacionadas
Application
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.
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.
Biochem/physiol Actions
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.
General description
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.
Other Notes
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.
Physical form
Supplied as a solution in 20 mM Tris, 0.8 M NaCl and 25% glycerol, pH 7.6
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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
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
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
Su Duy Nguyen et al.
Journal of lipid research, 53(10), 2115-2125 (2012-08-03)
HDL particles may enter atherosclerotic lesions having an acidic intimal fluid. Therefore, we investigated whether acidic pH would affect their structural and functional properties. For this purpose, HDL(2) and HDL(3) subfractions were incubated for various periods of time at different
Ananya Roy et al.
The Journal of biological chemistry, 289(1), 237-250 (2013-11-22)
During infection and tissue damage, virulence factors and alarmins are pro-inflammatory and induce activation of various immune cells including macrophages and mast cells (MCs). Activated MCs instantly release preformed inflammatory mediators, including several proteases. The chymase mouse mast cell protease
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