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10791156001

Roche

Endoproteinase Glu-C (V8 Protease)

from Staphylococcus aureus V8

Synonym(s):

V8 protease, protease v8

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About This Item

Enzyme Commission number:
UNSPSC Code:
23201100

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.

Specificity

Heat inactivation: Endoproteinase Glu-C is inactivated by boiling for ten minutes.

Application

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

Biochem/physiol Actions

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.

Storage and Stability

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_germany

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash


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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
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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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