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About This Item
UNSPSC Code:
12352200
NACRES:
NA.77
Form:
powder
Solubility:
water: 0.1 g/mL, clear, colorless
Storage temp.:
2-8°C
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
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.
Biochem/physiol Actions
Protease inhibitors: serine, cysteine and aspartic proteases, and metalloproteases
Phosphatase inhibitors: tyrosine, serine/threonine, acid and alkaline phosphatases
Phosphatase inhibitors: tyrosine, serine/threonine, acid and alkaline phosphatases
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.
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.
Physical form
Lyophilized powder that is water-soluble
Preparation Note
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.
Other Notes
Protease inhibitors:
- Bestatin hydrochloride
- Leupeptin
- Phosphoramidon disodium salt
- Pepstatin A
- Elastatinal
- Aprotinin
- Nafamostat mesylate
- Antipain
- Okadaic acid
- Sodium fluoride
- Sodium orthovanadate
- Bromotetramisole oxalate
- β-lactose
- DL-leucine
Signal Word
Warning
Hazard Statements
Precautionary 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
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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
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
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
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