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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.

Synonym(s):

Mass Spectrometry Safe Protease and Phosphatase Inhibitor Cocktail

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.77

product name

MS-SAFE Protease and Phosphatase Inhibitor,

description

for use with mammalian cell and tissue extract, lyophilized powder

Quality Level

form

powder

solubility

water: 0.1 g/mL, clear, colorless

storage temp.

2-8°C

General description

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.

Specificity

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.

Features and Benefits

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.

Components

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

Quantity

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.

Physical form

Lyophilized powder that is water-soluble

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
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)
Nina E Murugina et al.
The Journal of biological chemistry, 295(10), 3099-3114 (2020-02-02)
Upon activation with pathogen-associated molecular patterns, metabolism of macrophages and dendritic cells is shifted from oxidative phosphorylation to aerobic glycolysis, which is considered important for proinflammatory cytokine production. Fragments of bacterial peptidoglycan (muramyl peptides) activate innate immune cells through nucleotide-binding
Xuming Wang et al.
Molecular medicine reports, 11(5), 3375-3381 (2014-12-30)
The present study investigated the protein expression levels of cluster of differentiation (CD)95, caspase‑8, caspase‑3 and poly(ADP‑ribose) polymerase 1 (PARP1) in liver cancer and its association with clinical pathological parameters. The results demonstrated that the expression of CD95 correlated with

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