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MSSAFE

Sigma-Aldrich

Protease and Phosphatase Inhibitor Cocktail

MS-SAFE, powder, Protease inhibitors: serine, cysteine and aspartic proteases and metalloproteases. Phosphatase inhibitors: tyrosine, serine/threonine, acid and alkaline phosphatases.

Synonyme(s) :

Mass Spectrometry Safe Protease and Phosphatase Inhibitor Cocktail

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77

product name

MS-SAFE Protease and Phosphatase Inhibitor,

Description

for use with mammalian cell and tissue extract, lyophilized powder

Forme

powder

Solubilité

water: 0.1 g/mL, clear, colorless

Température de stockage

2-8°C

Description générale

Mass spectrometry (MS) compatible protease inhibitor cocktail and phosphatase inhibitor cocktail, with broad specificity for the inhibition of:
  • Serine, cysteine and aspartic proteases, and metalloproteases
  • Tyrosine, serine/threonine, acid and alkaline phosphatases
All inhibitors and fillers were chosen so as not to interfere with LC-MS analyses. Any inhibitors capable of covalent, irreversible protein modification were avoided. This cocktail is EDTA-free. All inhibitors were selected to allow facile downstream sample processing, such as immobilized metal affinity chromatography (IMAC) for His-tagged protein purification and, uniquely, phosphopeptide enrichment.

Spécificité

Protease inhibitors: serine, cysteine and aspartic proteases, and metalloproteases
Phosphatase inhibitors: tyrosine, serine/threonine, acid and alkaline phosphatases

Application

MS-SAFE Protease and Phosphatase Inhibitor has been used to measure ribosomal protein S6 kinase (S6K) activity.
Tested in mammalian cell lysates and liver tissue extracts. Designed for use in samples to be analyzed by mass spectrometry.

Caractéristiques et avantages

Comprehensive protease and phosphatase inhibitor cocktail for mass spectrometry analysis

Compatible with downstream sample processing such as His-tagged protein purification and phosphopeptide enrichment

Allows accurate measurement of protein activity and identification of phosphorylation sites.

Composants

Protease inhibitors:
  • Bestatin hydrochloride
  • Leupeptin
  • Phosphoramidon disodium salt
  • Pepstatin A
  • Elastatinal
  • Aprotinin
  • Nafamostat mesylate
  • Antipain
Phosphatase inhibitors
  • Okadaic acid
  • Sodium fluoride
  • Sodium orthovanadate
  • Bromotetramisole oxalate
Fillers
  • β-lactose
  • DL-leucine

Quantité

One vial makes 20 mL of 1× inhibitor cocktail working solution, using either water or extraction/lysis buffer. Alternatively, a 10× concentrated solution may be prepared by adding 2 mL of water or extraction/lysis buffer. This 10× solution may then be diluted 10-fold into extraction/lysis buffer as needed for a 1× working solution.

Forme physique

Lyophilized powder that is water-soluble

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Acute Tox. 4 Oral - Eye Irrit. 2 - Skin Irrit. 2

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Junguo Ma et al.
Chemosphere, 194, 773-783 (2017-12-19)
A previous study showed that microcystin-LR (MC-LR) exerted cytotoxicity and induced apoptosis in HepG2 cells. In the present study, we investigated whether oxidative stress-mediated p53/p21
Aberrant REDD1-mTORC1 responses to insulin in skeletal muscle from Type 2 diabetics.
Williamson, D.L., et al.
American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, 309, R855-R863 (2015)
S K Sreedharan et al.
The Biochemical journal, 316 ( Pt 3), 777-786 (1996-06-15)
1-trans-Epoxysuccinyl-L-leucylamido(4-guanidino)butane (E-64) was shown to inhibit beta-trypsin by a reversible competitive mechanism; this contrasts with the widely held view that E-64 is a class-specific inhibitor of the cysteine proteinases and reports in the literature that it does not inhibit a
Mark D Schuchard et al.
BioTechniques, 39(2), 239-247 (2005-08-25)
The inclusion of protease inhibitors in serum or plasma samples has been found to significantly impact the isoform profile of selected plasma proteins as seen on 2-dimensional electrophoresis (2-DE) gels. With the addition of a protease inhibitor cocktail, several human
Yumei Li et al.
Oncology letters, 14(6), 8035-8041 (2018-01-19)
Rhabdoid tumors, which tend to occur prior to the age of 2 years, are one of the most aggressive malignancies and have a poor prognosis due to the frequency of metastasis. Silibinin, a natural extract, has been approved as a

Contenu apparenté

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.

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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