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Protease Inhibitor Cocktail

for plant cell and tissue extracts, DMSO solution

MDL number:

Quality Level


DMSO solution

storage temp.


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Inhibits serine, cysteine, and aspartic proteases, metalloproteases, and aminopeptidases


1, 5 mL in glass bottle


Optimized and tested for use with plant tissue and cell extracts. Specific testing was done on plant seedling extracts from pea, bean, wheat, tobacco, and Arabidopsis, as well as leaf and root extracts from pea, wheat and tobacco.

Biochem/physiol Actions

This mixture contains individual components, including AEBSF, 1,10-Phenanthroline, Pepstatin A, Leupeptin, Bestatin, and E-64. Each component has specific inhibitory properties. AEBSF acts to inhibit serine proteases, including trypsin, chymotrypsin, and plasmin amongst others. Bestatin inhibits aminpeptidases. E-64 acts against cystein proteases. Leupeptin acts against both serine and cystein proteases. Pepstatin A inhibits acid proteases. 1,10-Phenanthroline acts against metalloproteases.


Pepstatin A


The cocktail should be stored at -20°C, where it will retain stability for two years.


One mL is recommended for the inhibition of proteases extracted from 30 g of plant tissue in a total volume of 100 ml.

Preparation Note

This product is supplied as a clear, faint pink solution in DMSO. One mL of solution is recommended for inhibition of protease activity in 100 mL of cell lysate from 30 g of various plant tissues or 10 g of baculovirus-infected cells. Extracts of plant seedlings from pea, bean, wheat, tobacco, and Arabidopsis have been tested. The roots of these plants have also been successfully tested.

Storage Class Code

10 - Combustible liquids



Flash Point(F)

185.0 °F - closed cup

Flash Point(C)

85 °C - closed cup

Certificate of Analysis

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Certificate of Origin

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Aurine Verkest et al.
The Plant cell, 17(6), 1723-1736 (2005-05-03)
Exit from the mitotic cell cycle and initiation of cell differentiation frequently coincides with the onset of endoreduplication, a modified cell cycle during which DNA continues to be duplicated in the absence of mitosis. Although the mitotic cell cycle and
Shugo Maekawa et al.
Frontiers in plant science, 9, 1177-1177 (2018-09-14)
The Brix domain is a conserved domain in several proteins involved in ribosome biogenesis in yeast and animals. In the Arabidopsis genome, six Brix domain-containing proteins are encoded; however, their molecular functions have not been fully characterized, as yet. Here
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Globally, avian influenza (AI) is a serious problem in poultry farming. Despite vaccination, the prevalence of AI in México highlights the need for new approaches to control AI and to reduce the economic losses associated with its occurrence in susceptible
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Proceedings of the National Academy of Sciences of the United States of America, 110(21), 8744-8749 (2013-05-08)
In animals and plants, pathogen recognition triggers the local activation of intracellular signaling that is prerequisite for mounting systemic defenses in the whole organism. We identified that Arabidopsis thaliana isoform CPK5 of the plant calcium-dependent protein kinase family becomes rapidly
Julia A Chekanova et al.
Cell, 131(7), 1340-1353 (2007-12-28)
The exosome complex plays a central and essential role in RNA metabolism. However, comprehensive studies of exosome substrates and functional analyses of its subunits are lacking. Here, we demonstrate that as opposed to yeast and metazoans the plant exosome core

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