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P8215

Sigma-Aldrich

Protease Inhibitor Cocktail

for use with fungal and yeast extracts, DMSO solution

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Synonym(s):
Protease Inhibitor Mix, Protease inhibitor
EC Number:
MDL number:

Quality Level

form

DMSO solution

storage temp.

−20°C

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This Item
P8340P8849P1860
Protease Inhibitor Cocktail for use with fungal and yeast extracts, DMSO solution

P8215

Protease Inhibitor Cocktail

Sigma-Aldrich

P8340

Protease Inhibitor Cocktail

Protease Inhibitor Cocktail for use in purification of Histidine-tagged proteins, DMSO solution

P8849

Protease Inhibitor Cocktail

Protease Inhibitor Cocktail for use in tissue culture media, DMSO solution

P1860

Protease Inhibitor Cocktail

Quality Level

300

Quality Level

300

Quality Level

300

Quality Level

200

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

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

Specificity

Inhibits serine, cysteine, aspartic, and metalloproteases.

Application

Protease Inhibitor Cocktail has been used as a component in:
  • FA buffer to wash spheroplasts to obtain an average DNA fragment size for chromatin immunoprecipitation (chip)
  • potassium phosphate buffer (pbs) to digest chitin
  • extraction buffer for grinding powdered mycelia for co-immunoprecipitation analysis

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.

Components

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.
This product is for R&D use only, not for drug, household, or other uses. Please consult the Material Safety Data Sheet for information regarding hazards and safe handling practices.

Quantity

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

Physical form

Solution in DMSO

pictograms

Exclamation markEnvironment

signalword

Warning

Hazard Classifications

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

188.6 °F

flash_point_c

87 °C


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Calcineurin subunits A and B interact to regulate growth and asexual and sexual development in Neurospora crassa
Tamuli R, et al.
Testing, 11(3), e0151867-e0151867 (2016)
Microbial biomass in compost during colonization of Agaricus bisporus
Vos AM, et al.
AMB Express, 7, 1-7 (2017)
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.
A genome-wide screen reveals a role for the HIR histone chaperone complex in preventing mislocalization of budding yeast CENP-A
Ciftci-Yilmaz S, et al.
Genetics, 210(1), 203-218 (2018)
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

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