Skip to Content
Merck
All Photos(3)

Key Documents

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

Sign Into View Organizational & Contract Pricing


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

Looking for similar products? Visit Product Comparison Guide

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Inkar Castellanos-Huerta et al.
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
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
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
Daniel Tran et al.
Nature communications, 8(1), 1009-1009 (2017-10-19)
Responses of cells to mechanical stress are thought to be critical in coordinating growth and development. Consistent with this idea, mechanically activated channels play important roles in animal development. For example, the PIEZO1 channel controls cell division and epithelial-layer integrity

Related Content

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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service