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Merck
CN

10791156001

Roche

Endoproteinase Glu-C (V8 Protease)

from Staphylococcus aureus V8

Synonym(s):

V8 protease, protease v8

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About This Item

EC Number:
UNSPSC Code:
23201100
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form

lyophilized (salt-free)

specific activity

20 U/mg

mol wt

30 kDa

packaging

pkg of 2 mg

manufacturer/tradename

Roche

optimum pH

8.0-8.5

General description

Approximately 20 U/mg lyophilizate at +25°C with Z-Phe-Leu-Glu-4-nitranilide as the substrate (approximately 500 U/mg lyophilizate at +37°C with casein as the substrate).
At 25 °C with Z-Phe-Leu-Glu-4-nitranilide as the substrate (approximately 500 U/mg lyophilizate at 37 °C with casein as the substrate).
Endoproteinase Glu-C is a Staphylococcal serine proteinase. Its inhibitors are DFP, α2-macroglobulin and TLCK.

Application

Use Endoproteinase Glu-C (V8 Protease) for protein structure analysis and for sequence analysis.

Biochem/physiol Actions

Heat inactivation: Endoproteinase Glu-C is inactivated by boiling for ten minutes.
Endoproteinase Glu-C specifically hydrolyzes peptide and ester bonds at the carboxylic side of Glu, or both Glu and Asp, depending on the buffer used.

Preparation Note

Activator: The enzyme has its maximal activity in presence of SH-reagents
Working concentration: 1 to 5 mM
Working solution: Recommended solvent is 50 mM ammonium acetate pH 4.0 (2 mg/ml).
Storage conditions (working solution): -15 to -25 °C
The enzyme (2 mg/ml in 50 mM ammonium acetate, pH 4.0) is stable for at least one month, frozen in aliquots and thawed only once.
Store at 2 to 8 °C. (Store dry!)

Other Notes

For life science research only. Not for use in diagnostic procedures.

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash

Regulatory Information

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Neha Garg et al.
Biopolymers, 106(6), 834-842 (2016-05-15)
The biosynthesis of the class II lanthipeptide geobacillin II was reconstituted in vitro. The purified precursor peptide was modified by the lanthipeptide synthetase GeoM at temperatures ranging between 37 and 80°C demonstrating the thermostability of the enzyme. Geobacillin II shares
Marion Avril et al.
PLoS pathogens, 9(6), e1003430-e1003430 (2013-07-05)
During blood stage infection, Plasmodium falciparum infected erythrocytes (IE) bind to host blood vessels. This virulence determinant enables parasites to evade spleen-dependent killing mechanisms, but paradoxically in some cases may reduce parasite fitness by killing the host. Adhesion of infected
Rosalynn C Molden et al.
Current protocols in protein science, 77, 23-23 (2014-08-02)
Histones are chromatin proteins that are highly modified with many different types of post-translational modifications. These modifications act in concert to regulate a number of chromatin-related processes. However, identification and quantification of co-occurring histone post-translational modifications is challenging because there
Petr Pompach et al.
Journal of proteome research, 11(3), 1728-1740 (2012-01-14)
Glycoproteins fulfill many indispensable biological functions, and changes in protein glycosylation have been observed in various diseases. Improved analytical methods are needed to allow a complete characterization of this complex and common post-translational modification. In this study, we present a
Tianshi Wang et al.
Molecular cell, 75(4), 823-834 (2019-07-16)
Sirt3, as a major mitochondrial nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, is required for mitochondrial metabolic adaption to various stresses. However, how to regulate Sirt3 activity responding to metabolic stress remains largely unknown. Here, we report Sirt3 as a SUMOylated protein in

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