P8215
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
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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
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
signalword
Warning
hcodes
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
Certificates of Analysis (COA)
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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 cell, 50(2), 273-280 (2013-03-19)
The ring-shaped complex PCNA coordinates DNA replication, encircling DNA to act as a polymerase clamp and a sliding platform to recruit other replication proteins. PCNA is loaded onto DNA by replication factor C, but it has been unknown how PCNA
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
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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