Chymase, Recombinant, Human (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.\n\nSource: \nThe recombinant human chymase encoded by CMA1 gene (rhChymase, residues 1-247, P23946) was expressed with a C-terminal 10X His tag in a mouse myeloma cell line, NS0. \n\nMolecular Mass:\nThe secreted, purified rhChymase has an N-terminal sequence of G20 EIIGGTE, which corresponds to the pro form. The 238 amino acid His-tagged protein predicts a molecular mass of 27kD and migrates with an apparent molecular mass of approximately 38kD in SDS-PAGE under reducing conditions. \n\nEndotoxin Level: \n< 1.0 EU per 1 microg of the protein as determined by the LAL method. \n\nActivity: \nMeasured by its ability to cleave a fluorogenic peptide substrate, N-Ala-Ala-Pro-Phe-AMC. The specific activity, measured with 100 microM substrate and 100 ng activated enzyme in 100 microL of 20 mM Tris, 2.0 M KCl, 0.02 % Triton X-100, pH 9.0 at room temperature, is > 80 pmoles/min/microg. \n\nStorage:\nSamples are stable for up to six months at -20 degrees C in a manual defrost freezer after the date of receipt. After receiving, this protein can be aliquoted and stored at above temperature for up to six months without a significant loss of activity. Avoid repeated freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

M2414-01C

Size

10ug

Form

Supplied as a liquid in 25mM HEPES, 1.0M NaCl, pH 7.5.

Purity

(same/more than) 90%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Caughey, G.H. 2004, in Handbook of Proteolytic Enzymes (ed. Barrett, et al.), pp. 1531 - 1535, Academic Press, San Diego. \n2. Murakami, M. et al., 1995, J. Biol. Chem. 270:2218. \n3. Miyazaki, M. and Takai, S. 2006, J. Pharmacol. Sci. 100:391. \n4. Nakajima, M. and Naya, N. 2002, Jpn. J. Pharmacol. 90:206.