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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

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

Certificates of Analysis (COA)

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M Malkoski et al.
Antimicrobial agents and chemotherapy, 45(8), 2309-2315 (2001-07-14)
Caseinomacropeptide (CMP) is a heterogeneous C-terminal fragment (residues 106 to 169) of bovine milk kappa-casein composed of glycosylated and phosphorylated forms of different genetic variants. We have demonstrated that CMP has growth-inhibitory activity against the oral opportunistic pathogens Streptococcus mutans
R Pietropaolo et al.
The Journal of general virology, 80 ( Pt 7), 1807-1816 (1999-07-28)
Annexin II has been identified as a human cytomegalovirus (HCMV)-binding protein, shown to be a component of purified virions and proposed as a cellular receptor for the virus. In addition, annexin II is capable of associating with the major HCMV
Q Xu et al.
The Biochemical journal, 341 ( Pt 3), 733-737 (1999-07-27)
A galactose-binding lectin isolated from the venom of Trimeresurus stejnegeri is a homodimer C-type lectin. The cloned cDNA encoding the monomer of Trimeresurus stejnegeri lectin (TSL) was sequenced and found to contain a 5'-end non-coding region, a sequence which encodes
Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
Giganti D et al.
Nature Chemical Biology, 11, 16-16 (2015)
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
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