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P8215

Sigma-Aldrich

Protease Inhibitor Cocktail

DMSO solution, for the inhibition of serine, cysteine, aspartic and metalloproteases, for use with fungal and yeast extracts, DMSO solution

Synonym(s):

Protease Inhibitor Mix, Protease inhibitor

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About This Item

EC Number:
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.54

product name

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

Quality Level

form

DMSO solution

storage temp.

−20°C

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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

Signal Word

Warning

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

WGK

WGK 3

Flash Point(F)

188.6 °F

Flash Point(C)

87 °C


Certificates of Analysis (COA)

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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
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
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)
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.

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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.

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

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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