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Protease Inhibitor Cocktail

for use with fungal and yeast extracts, DMSO solution

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Protease inhibitor
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DMSO solution

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storage temp.


storage temp.


storage temp.


storage temp.


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Quality Level


Quality Level


Quality Level


General description

The Protease Inhibitor Cocktail for fungal and yeast extracts is a mixture of protease inhibitors in DMSO solution.

The cocktail has a broad specificity and inhibits serine, cysteine, aspartic, and metalloproteases.


Inhibits serine, cysteine, aspartic, and metalloproteases.


The cocktail has been optimized and tested for use on fungal and yeast samples, specifically on Saccharomyces cerevisiae cells.

One mL of the cocktail is recommended for the inhibition of proteases extracted from 20 g of yeast.

Features and Benefits

Broad specificity: inhibits a wide range of proteases, providing comprehensive protection to fungal and yeast extracts.

Tested on Saccharomyces cerevisiae cells: the cocktail has been optimized for use on this commonly studied yeast strain.

Convenient packaging: available in a 1 or 5 mL glass bottle for easy handling and storage.

Ready-to-use solution: the cocktail is supplied in DMSO solution for immediate use in protease inhibition assays.

Effective inhibition: each component in the cocktail has been carefully selected for its specific inhibitory properties, ensuring reliable and consistent results.


AEBSF, 100 mM
E-64, 1.4 mM
Pepstatin A, 2.2 mM
1,10-Phenanthroline, 500 mM

Other Notes

Mixture of protease inhibitors with broad specificity for the inhibition of serine, cysteine, aspartic and metallo-proteases. Contains 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF), pepstatin A, E-64, and 1,10-phenanthroline.


One mL is recommended for the inhibition of proteases extracted from 20 g of yeast.

Physical form

Solution in DMSO


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Hazard Statements

Hazard Classifications

Acute Tox. 4 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Eye Irrit. 2 - Skin Irrit. 2

Storage Class Code

10 - Combustible liquids



Flash Point(F)

188.6 °F

Flash Point(C)

87 °C

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Jin H Lee et al.
Virology, 378(2), 347-354 (2008-07-08)
In this study we have defined protein-protein interactions between the structural proteins of herpes simplex virus type 1 (HSV-1) using a LexA yeast two-hybrid system. The majority of the capsid, tegument and envelope proteins of HSV-1 were screened in a
Wei Xie et al.
Molecular biology of the cell, 20(14), 3317-3329 (2009-05-22)
Endoplasmic reticulum (ER) quality control mechanisms monitor the folding of nascent polypeptides of the secretory pathway. These are dynamic processes that retain folding proteins, promote the transport of conformationally mature proteins, and target misfolded proteins to ER-associated degradation (ERAD) pathways.
Elena Pérez-Nadales et al.
The Plant cell, 23(3), 1171-1185 (2011-03-29)
Fungal pathogenicity in plants requires a conserved mitogen-activated protein kinase (MAPK) cascade homologous to the yeast filamentous growth pathway. How this signaling cascade is activated during infection remains poorly understood. In the soil-borne vascular wilt fungus Fusarium oxysporum, the orthologous
R Koszul et al.
Cell, 133(7), 1188-1201 (2008-07-01)
Chromosome movement is prominent during meiosis. Here, using a combination of in vitro and in vivo approaches, we elucidate the basis for dynamic mid-prophase telomere-led chromosome motion in budding yeast. Diverse findings reveal a process in which, at the pachytene
Takashi Kubota et al.
Molecular & cellular proteomics : MCP, 10(7), M110-M110 (2011-04-21)
Yeast cells lacking Ctf18, the major subunit of an alternative Replication Factor C complex, have multiple problems with genome stability. To understand the in vivo function of the Ctf18 complex, we analyzed chromatin composition in a ctf18Δ mutant using the

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