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324713

Sigma-Aldrich

Endoproteinase Glu-C, Excision Grade, Staphylococcus aureus

Synonym(s):

Endoproteinase Glu-C, Excision Grade, Staphylococcus aureus, V8 Protease

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.54

biological source

Staphylococcus aureus

Quality Level

grade

Proteomics Grade

form

lyophilized

specific activity

≥10 units/mg protein

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

shipped in

ambient

storage temp.

2-8°C

General description

Native endoproteinase Glu-C from Staphylococcus aureus. Serine protease that specifically hydrolyzes peptide bonds at the carboxylic side of glutamic acid and aspartic acid residues. Inhibited by DFP and α2-macroglobulin.
Native endoproteinase Glu-C from Staphylococcus aureus. Serine protease that specifically hydrolyzes peptide bonds at the carboxylic side of glutamic acid and aspartic acid residues. Inhibited by DFP and α2-macroglobulin. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.

Warning

Toxicity: Harmful (C)

Unit Definition

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Z-Phe-Leu-Glu-pNA per min at 25°C, pH 7.8.

Reconstitution

Following reconstitution, aliquot and freeze (-20°C) for long term storage or refrigerate (4°C) for short term storage. Stock solutions are stable for up to 2 days at 4°C or for up to 1 month at -20°C.

Other Notes

Houmard, J., and Drapeau, G.R. 1972. Proc. Natl. Acad. Sci. USA69, 3506.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Victoria L Stefanelli et al.
Matrix biology : journal of the International Society for Matrix Biology, 82, 86-104 (2019-04-21)
The extracellular matrix (ECM) microenvironment is increasingly implicated in the instruction of pathologically relevant cell behaviors, from aberrant transdifferentation to invasion and beyond. Indeed, pathologic ECMs possess a panoply of alterations that provide deleterious instructions to resident cells. Here we

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