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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

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


Certificates of Analysis (COA)

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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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