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C8118

Sigma-Aldrich

Chymase human

recombinant, expressed in Pichia pastoris

Synonym(s):

Mast cell protease I

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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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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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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