C8118
Chymase human
recombinant, expressed in Pichia pastoris
Synonym(s):
Mast cell protease I
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
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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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
Storage Class
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)
Regulatory Information
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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
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
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
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
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
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