Select a Size
All Photos(3)
About This Item
form:
DMSO solution
solubility:
water: soluble
storage temp.:
−20°C
Product Name
Protease Inhibitor Cocktail, for plant cell and tissue extracts, DMSO solution
form
DMSO solution
solubility
water: soluble
storage temp.
−20°C
Quality Level
Looking for similar products? Visit Product Comparison Guide
Related Categories
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
Inhibits serine, cysteine, and aspartic proteases, metalloproteases, and aminopeptidases
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.
Disclaimer
The cocktail should be stored at -20°C, where it will retain stability for two years.
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
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
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.
Other Notes
AEBSF
Bestatin
E-64
Leupeptin
Pepstatin A
1,10-Phenanthroline
Bestatin
E-64
Leupeptin
Pepstatin A
1,10-Phenanthroline
Preparation Note
One mL is recommended for the inhibition of proteases extracted from 30 g of plant tissue in a total volume of 100 ml.
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
10 - Combustible liquids
wgk
WGK 1
flash_point_f
185.0 °F - closed cup
flash_point_c
85 °C - closed cup
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in 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
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
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
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