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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

UNSPSC Code:
23201100
EC Number:
NACRES:
NA.54
Specific activity:
20 U/mg
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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

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash

Regulatory Information

常规特殊物品

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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
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
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



Global Trade Item Number

SKUGTIN
1079115600104061838676719