Human Chymase/CMA1 Antibody Summary
Gly20-Asn247
Accession # P23946
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Human Chymase/CMA1 by Western Blot. Western blot shows lysates of human small intestine tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human Chymase/CMA1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4099) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Chymase/CMA1 at approximately 28 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Reconstitution Calculator
Preparation and Storage
- 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: Chymase/CMA1
Chymases are a group of chymotrypsin-like serine proteases secreted by mast cells (1). They are synthesized as inactive precursors containing a 2-residue propeptide, which needs to be removed by dipeptidyl peptidase I/cathepsin C for the enzymatic activity (2). Human Chymase encoded by the CMA1 gene is known to be involved in hypertention and heart failure through its ability to convert angiotensin I (Ang I) to angiotensin II (Ang II), which plays a key role in the regulation of arterial pressure (3). In addition, it is also important in physiological and pathological conditions including inflammation, fibrosis and processing of cytokines (4). Therefore, designing a specific inhibitor for Chymase activity has been a pharmacologic strategy to develop therapeutic agents.
- Caughey, G.H. (2004) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. ed. p. 1531, Academic Press, San Diego.
- Murakami, M. et al. (1995) J. Biol. Chem. 270:2218.
- Miyazaki, M. and S. Takai (2006) J. Pharmacol. Sci. 100:391.
- Nakajima, M. and N. Naya (2002) Jpn. J. Pharmacol. 90:206.
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