P8215
Protease Inhibitor Cocktail
DMSO solution, for the inhibition of serine, cysteine, aspartic and metalloproteases, for use with fungal and yeast extracts, DMSO solution
Sinonimo/i:
Protease Inhibitor Mix, Protease inhibitor
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Prodotti consigliati
Nome del prodotto
Cocktail di inibitori delle proteasi, for use with fungal and yeast extracts, DMSO solution
Livello qualitativo
Stato
DMSO solution
Solubilità
water: soluble
Temperatura di conservazione
−20°C
Cerchi prodotti simili? Visita Guida al confronto tra prodotti
Descrizione generale
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.
Specificità
Inhibits serine, cysteine, aspartic, and metalloproteases.
Applicazioni
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
Caratteristiche e vantaggi
- 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.
Componenti
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
Altre note
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.
Quantità
One mL is recommended for the inhibition of proteases extracted from 20 g of yeast.
Stato fisico
Solution in DMSO
Prodotti correlati
N° Catalogo
Descrizione
Determinazione del prezzo
Avvertenze
Warning
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Acute Tox. 4 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Eye Irrit. 2 - Skin Irrit. 2
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
188.6 °F
Punto d’infiammabilità (°C)
87 °C
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
I clienti hanno visto anche
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.
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.