P6181
Glu-C Protease
Cleaves at glutamic acid residues, suitable for Mass Spectrometry, from Staphylococcus aureus V8
Synonyme(s) :
V8 Protease
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
200-350-6
MDL number:
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Endoproteinase Glu-C from Staphylococcus aureus V8, suitable for protein sequencing, lyophilized powder
grade
Proteomics Grade
form
lyophilized powder
analyte chemical class(es)
amino acids
suitability
suitable for protein sequencing
storage temp.
−20°C
Quality Level
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Catégories apparentées
Application
Endoproteinase Glu-C from Staphylococcus aureus V8 has been used for:
- obtaining proteolytic cleavage fragments of the S-layer protein (from Bacillus stearothermophilus ATCC 12980) to perform affinity studies.
- the enzymatic cleavage of native VSTx-3 (voltage sensor toxin 3) peptide for its sequence determination.
- limited proteolysis of recombinant purified PimA (phosphatidylinositol mannosyltransferase).
- the digestion of glycosylated hemoglobin for isotope dilution liquid chromatography-tandem mass spectrometry analysis.
Biochem/physiol Actions
Endoproteinase Glu-C from Staphylococcus aureus strain V8 is a serine endoprotease, which hydrolyzes peptide bonds at the carboxyl side of glutamyl and aspartyl residues. The specificity of Glu-C is dependent upon the buffer and pH employed as well as the structure around the potential cleavage site. In ammonium acetate (pH 4.0) or ammonium bicarbonate (pH 7.8), the enzyme preferentially cleaves glutamyl bonds; whereas, in phosphate buffer (pH 7.8) Glu-C will cleave at either site. Glu-C is reported to be active in the presence of 0.2% SDS (sodium dodecyl sulfate) and in 4.0M urea.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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M Malkoski et al.
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Giganti D et al.
Nature Chemical Biology, 11, 16-16 (2015)
Q Xu et al.
The Biochemical journal, 341 ( Pt 3), 733-737 (1999-07-27)
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Daniel B Williamson et al.
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