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P6181

Sigma-Aldrich

Endoproteinase Glu-C from Staphylococcus aureus V8

suitable for protein sequencing, lyophilized powder

Synonym(s):

V8 Protease

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About This Item

CAS Number:
66676-43-5
Enzyme Commission number:
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

Signal Word

Danger

Hazard Statements

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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X. Wang et al.
Plant physiology, 111(2), 441-445 (1996-06-01)
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and a 66-kD protein were co-purified from solubilized microsomal preparations of the green alga Botryococcus braunii by Green A agarose, sucrose density gradient, MonoQ, and gel filtration. The 66-kD protein remained intact after 6 M urea treatment
The Protein Protocols Handbook (1996)
M Jarosch et al.
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
Kenneth AW
Human Genome Methods (1997)
Mechanism of acylphosphatase inactivation by Woodward's reagent K.
Paoli, P., et al.
The Biochemical Journal, 855-861, 855-861 (1997)
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