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Chymase human

recombinant, expressed in Pichia pastoris

Mast cell protease I
CAS Number:
Enzyme Commission number:
MDL number:


expressed in Pichia pastoris

Quality Level



specific activity

≥40 units/mg protein

mol wt

~37 kDa by SDS-PAGE


125-400 μg/mL

UniProt accession no.


diagnostic assay manufacturing

shipped in

dry ice

storage temp.


Gene Information

human ... CMA1(1215)

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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



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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