Tryptase, Human Lung

Native tryptase from human lung. Tryptase is a serine protease stored in mast cell granules. A tetrameric enzyme composed of four non-covalently bound subunits. Each subunit is reported to contain one active site. Reported to upregulate neoangiogenesis in carcinogenesis of the uterine cortex. Tryptase is also an important mediator of allergic reactions that activates G-protein-coupled receptors through proteolysis, thus amplifying histamine release.

Native tryptase from human lung. Tryptase is a serine protease stored in mast cell granules. A tetrameric enzyme composed of four non-covalently bound subunits. Each subunit is reported to contain one active site. Tryptase is an important mediator of allergic reactions that activates G-protein-coupled receptors through proteolysis, thus amplifying histamine release.

Toxicity: Irritant (B)

One unit is defined as the amount of enzyme that gives a change of 1 absorbance per min at 410 nm using N-benzoyl-Phe-Val-Arg-pNA as a substrate in 30 min at 25°C.

In 1 M NaCl, 50 mM NaOAc, 50 µM heparin, pH 5.0.

Prepared from tissue that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Following initial thaw, aliquot and freeze (-20°C).

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Molino, M., et al. 1997. J. Biol. Chem. 272, 4043.
Schwartz, L.B., and Bradford, T.R. 1986. J. Biol. Chem. 261, 7372.

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