P9599
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
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
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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
Regulatory Information
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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
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
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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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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