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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:
UNSPSC Code:
12352200
NACRES:
NA.77

product name

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

Quality Level

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.

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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The Plant cell, 17(6), 1723-1736 (2005-05-03)
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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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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

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