Seleccione un Tamaño
About This Item
form:
DMSO solution
solubility:
water: soluble
storage temp.:
−20°C
Nombre del producto
Cóctel de inhibidores de proteasas, for use with fungal and yeast extracts, DMSO solution
form
DMSO solution
solubility
water: soluble
storage temp.
−20°C
Quality Level
¿Está buscando productos similares? Visita Guía de comparación de productos
Categorías relacionadas
Other Notes
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.
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
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.
Physical form
Solution in DMSO
Preparation Note
One mL is recommended for the inhibition of proteases extracted from 20 g of yeast.
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.
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
Biochem/physiol Actions
Inhibits serine, cysteine, aspartic, and metalloproteases.
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.
signalword
Warning
hcodes
Hazard Classifications
Acute Tox. 4 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Eye Irrit. 2 - Skin Irrit. 2
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 3
flash_point_f
188.6 °F
flash_point_c
87 °C
Elija entre una de las versiones más recientes:
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
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
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)
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.
Microbial biomass in compost during colonization of Agaricus bisporus
Vos AM, et al.
AMB Express, 7, 1-7 (2017)
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
Contenido relacionado
Datasheet
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico
