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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.

Sinónimos:

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

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
GHS07

signalword

Warning

Hazard Classifications

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
Chandresh R Gajera et al.
Journal of neuroscience methods, 312, 73-83 (2018-11-23)
Synaptic alterations, especially presynaptic changes, are cardinal features of neurodegenerative diseases and strongly correlate with cognitive decline. We report "Mass Synaptometry" for the high-dimensional analysis of individual human synaptosomes, enriched nerve terminals from brain. This method was adapted from cytometry
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
Michael J Workman et al.
International journal of molecular sciences, 22(1) (2021-01-06)
Human intestinal organoids (HIOs) are increasingly being used to model intestinal responses to various stimuli, yet few studies have confirmed the fidelity of this modeling system. Given that the interferon-gamma (IFN-γ) response has been well characterized in various other cell
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Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Protease Inhibitor Selection: Avoid Protein Loss 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.

Protease Inhibitor Selection: Avoid Protein Loss 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.

Protease Inhibitor Selection: Avoid Protein Loss 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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