Chymostatin microbial | Sigma-Aldrich

Properties

Related Categories	A to C, Apoptosis Enzymes, Application Index, Bioactive Small Molecules, Biochemicals and Reagents, Broad Spectrum Inhibitors of Proteolytic Enzyme Classes, C-CH, Cathepsin B, Cathepsin D, Cathepsin G, Cathepsin/Granzyme Inhibitors & Substrates, Cell Biology, Cell Signaling Enzymes, Cell Signaling and Neuroscience, Chymotrypsin, α-, Chymotrypsin, alpha-, Core Bioreagents, Cysteine Protease Inhibitors, Enzyme Inhibitors, Enzyme Inhibitors by Enzyme, Enzymes, Inhibitors, and Substrates, Inhibitors, Life Science Reagents for Protein Expression and Purification, Lysosomal Proteases, Native Protein Sample Preparation, P to Q, Papain, Peptides and Proteins, Peptides for Cell Biology, Protease Inhibitor Specificity Index, Protease Inhibitors, Proteasome, Calpain and Lysosomal Proteases, Proteomics, Research Essentials, Serine Protease Inhibitors More...
biological source	microbial
solubility	DMSO: soluble10 mM (Stock solutions stable for months at −20 °C.)
storage temp.	−20°C

Description

Biochem/physiol Actions

Chymostatin is a strong inhibitor of many proteases, including chymotrypsin, papain, chymotrypsin-like serine proteinases, chymases, and lysosomal cysteine proteinases such as cathepsins A,B,C, B, H, and L. It weakly inhibits human leucocyte elastase. It is effective at a final concentration of 100 to 200 μg/ml (10 to 100 μM). Chymostatin is often included in protease inhibitor cocktails used with plant extracts.

Inhibits the lysosomal proteinase cathepsin B, and the soluble Ca²⁺-activated proteinase.¹ Many young plant tissues express a chomostatin-sensitive serine protease.²

Other Notes

A mixture of A (major), B and C components. A: X=Leu; B: X=Val; C: X=Ile
chymostatin A MW = 607.7
chymostatin B MW = 593.7
chymostatin C MW = 607.7

Preparation Note

Solubility testing in glacial acetic acid at 10 mg/ml yields a clear solution, which is usually colorless, but can be yellow in appearance. It is reportedly also soluble in DMSO; only slightly soluble in water and short-chain alcohols; insoluble in ethyl acetate, butyl acetate, ether, hexane, and petroleum ether. Stock solutions (10 mM) can be prepared in DMSO and are stable for months at -20 °C. Stock solutions can also be made in 0.1 M HCl. Dilute solutions (10-100 μM) are only stable for several hours, due to oxidation of the terminal aldehyde.

Application

Chymostatin has been used in a study that determined that molecular calculations are useful for evaluating the interactions between ligands, including inhibitors and homologous enzymes, in docking models. Chymostatin has also been used in a study to investigate the norovirus protease as an attractive target for antiviral drug development.

Price and Availability

Related Papers

Structures and activities of protease inhibitors of microbial origin. Umezawa, H. Meth. Enzymol. 45, 678, (1976)

Documents

Certificate of Analysis

Certificate of Origin

C7268 - Product Information Sheet (56 KB)

Safety Information

Personal Protective Equipment	Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
WGK Germany	3
RTECS	GC3047700

Technical information & documentation associated with this product is available in the Safety & Documentation tab.

Papers

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Beynon, R.J. and Bond, J.S., ed. Proteolytic Enzymes: A Practical Approach New York, NY , (1989), 207,243

Levy, M.R. and Chou, S.C. Biochim. Biophys. Acta 334, 423, (1974)

Structures and activities of protease inhibitors of microbial origin. Umezawa, H. Meth. Enzymol. 45, 678, (1976)

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The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin. Feinstein, G., et al. Biochim. Biophys. Acta 429, 925, (1976)

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Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay Chang, K., et al. Virology 423, 125-33, (2012)

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Comparative analysis of binding energy of chymostatin with human cathepsin A and its homologous proteins by molecular orbital calculation Yoshida, T., et al. J. Chem. Inf. Model. 46, 2093-103, (2012)

Cordysobin, a novel alkaline serine protease with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Cordyceps sobolifera Wang, S., et al. J. Biosci. Bioeng. 113(1), 42-7, (2011)

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