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P9599

Sigma-Aldrich

Protease Inhibitor Cocktail

DMSO solution, for the inhibition of serine, cysteine, aspartic, metalloproteases and aminopeptidases, for plant cell and tissue extracts, DMSO solution

Synonym(s):

Protease Inhibitor Mix

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About This Item

MDL number:
MFCD00677817
UNSPSC Code:
12352200
NACRES:
NA.77

product name

Protease Inhibitor Cocktail, for plant cell and tissue extracts, DMSO solution

Quality Level

300

form

DMSO solution

storage temp.

−20°C

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General description

Our Protease Inhibitor Cocktail is a mixture of individual components optimized and tested for use with plant tissue and cell extracts. The cocktail contains a broad specificity of inhibitory properties including serine, cysteine, aspartic and metalloproteases, and aminopeptidases. The individual components include AEBSF, 1,10-Phenanthroline, Pepstatin A, Leupeptin, Bestatin, and E-64.

Specificity

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

Application

This product has been specifically tested on plant seedling extracts from pea, bean, wheat, tobacco, and Arabidopsis, as well as leaf and root extracts from pea, wheat, and tobacco. The recommended quantity is one mL of solution for the inhibition of protease activity in 100 mL of cell lysate from 30 g of various plant tissues or 10 g of baculovirus-infected cells.

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.

Features and Benefits

Contains a broad specificity of inhibitory properties including serine, cysteine, aspartic and metalloproteases, and aminopeptidases

Optimized and tested for use with plant tissue and cell extracts

Specifically tested on plant seedling extracts from pea, bean, wheat, tobacco, and Arabidopsis, as well as leaf and root extracts from pea, wheat, and tobacco

One mL of solution is recommended for the inhibition of protease activity in 100 mL of cell lysate from 30 g of various plant tissues or 10 g of baculovirus-infected cells

Components

AEBSF
Bestatin
E-64
Leupeptin
Pepstatin A
1,10-Phenanthroline

Caution

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

Quantity

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

185.0 °F - closed cup

Flash Point(C)

85 °C - closed cup

Certificates of Analysis (COA)

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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
Birgit Agne et al.
The Journal of biological chemistry, 284(13), 8670-8679 (2009-02-04)
The heterotrimeric Toc core complex of the chloroplast protein import apparatus contains two GTPases, Toc159 and Toc34, together with the protein-conducting channel Toc75. Toc159 and Toc34 are exposed at the chloroplast surface and function in preprotein recognition. Together, they have
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Avian diseases, 60(4), 784-791 (2016-12-03)
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
Ullrich Dubiella et al.
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
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
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Protease Inhibitor Selection: Avoid Protein Loss in Sample Prep

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Protease Inhibitor Selection: Avoid Protein Loss in Sample Prep

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Protease Inhibitor Selection: Avoid Protein Loss in Sample Prep

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

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