This product, Chymase human, is an active form with activity specifications of ≥40 units/mg protein, indicating it is a mature form. The sequence information is proprietary and not available.
C8118
Chymase human
recombinant, expressed in Pichia pastoris
Synonym(s):
Mast cell protease I
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50 μG
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
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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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Related Categories
1 of 4
This Item | SAB5700983 | MAB1254 | MAB1254B |
|---|---|---|---|
| specific activity ≥40 units/mg protein | specific activity - | specific activity - | specific activity - |
| Gene Information human ... CMA1(1215) | Gene Information human ... CMA1(1215) | Gene Information human ... CMA1(1215) | Gene Information human ... CMA1(1215) |
| application(s) diagnostic assay manufacturing | application(s) - | application(s) - | application(s) - |
| recombinant expressed in Pichia pastoris | recombinant - | recombinant - | recombinant - |
| concentration 125-400 μg/mL | concentration 1.1 mg/mL | concentration 2.4 mg/mL | concentration - |
| form liquid | form liquid | form - | form - |
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.[1]
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
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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
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
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
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
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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Instructions
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CMA1 has a pro form starting at amino acid 20 and a mature form starting at amino acid 22. Can you tell me which form this is or the N-term origin?
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