C8118
Chymase human
recombinant, expressed in Pichia pastoris
Synonym(s):
Mast cell protease I
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in Pichia pastoris
Quality Level
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
Gene Information
human ... CMA1(1215)
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Related Categories
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.
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.
Physical properties
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.
Unit Definition
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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
S Takai et al.
Clinica chimica acta; international journal of clinical chemistry, 265(1), 13-20 (1997-11-14)
A chymostatin-sensitive angiotensin II-generating enzyme was found in human gastroepiploic arteries. The enzyme was purified using heparin affinity and gel filtration columns. The molecular mass of the purified enzyme was 30 kDa, and the optimum pH was between 7.5 and
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
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
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
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