Detection of Mouse Mast Cell Protease‑1/Mcpt1 by Western Blot. Western blot shows lysates of mouse small intestine tissue. PVDF Membrane was probed with 1 µg/mL of Mouse Mast Cell Protease‑1/Mcpt1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5146) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Mast Cell Protease‑1/Mcpt1 at approximately 30 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.
Preparation and Storage
Sterile PBS to a final concentration of 0.2 mg/mL.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Mast Cell Protease-1/Mcpt1
Mast cell protease-1 (Mcpt1), also known as beta ‑chymase, is a member of the Chymase family of chymotrypsin-like serine proteases (1). mMcpt1 is a mast cell protease predominantly expressed in intestinal mucosal mast cells where it promotes mucosal permeability in intestinal allergic hypersensitivity reactions (2). Its activation is completed by the removal of a two residue N‑terminal propeptide by a dipeptidyl peptidase (Cathepsin C) (3). Like human alpha ‑Chymase, Mcpt1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure (4). Studies have shown that specific chymase inhibitors are able to diminish the development of abdominal aortic aneurysm and reduce the adhesion formation after cardiac surgery in hamsters (5, 6). Therefore, the development of specific inhibitors of chymase activity has been a pharmacologic strategy to develop therapeutic agents.
Caughey, G.H. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.), p. 1531 Academic Press, San Diego.
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Murakami, M. et al. (1995) J. Biol. Chem. 270:2218.
Saito, K. et al. (2003) Biochem. Biophys. Res. Commun. 302:773.
Tsunemi, K. et al. (2004) J. Pharmacol. Exp. Ther. 309:879.
Soga, Y. et al. (2004) J. Thorac. Cardiovasc. Surg. 127:72.
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