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P6181

Sigma-Aldrich

Endoproteinase Glu-C from Staphylococcus aureus V8

suitable for protein sequencing, lyophilized powder

Sinónimos:

V8 Protease

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About This Item

Número de CAS:
66676-43-5
Comisión internacional de enzimas:
3.4.21.19 (BRENDA, IUBMB)
EC Number:
200-350-6
MDL number:
MFCD01324998
UNSPSC Code:
12352204
NACRES:
NA.54

grade

Proteomics Grade

Quality Level

200

form

lyophilized powder

analyte chemical class(es)

amino acids

suitability

suitable for protein sequencing

storage temp.

−20°C

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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.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Certificados de análisis (COA)

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The Protein Protocols Handbook (1996)
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Microbiology (Reading, England), 146 ( Pt 2), 273-281 (2000-03-09)
The cell surface of Bacillus stearothermophilus ATCC 12980 is completely covered with an oblique S-layer lattice. To investigate sequence identities and a common structure-function relationship in S-layer proteins of different B. stearothermophilus wild-type strains, the nucleotide sequence encoding the S-layer
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