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Merck

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:
Numéro CE :
eCl@ss:
32160410
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Nom du produit

Endoproteinase Glu-C from Staphylococcus aureus V8, suitable for protein sequencing, lyophilized powder

grade

Proteomics Grade

Quality Level

form

lyophilized powder

analyte chemical class(es)

amino acids

suitability

suitable for protein sequencing

storage temp.

−20°C

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.


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pictograms

Health hazard

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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Contenu apparenté


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
Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
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)
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



Numéro d'article de commerce international

RéférenceGTIN
P6181-50UG04061835574698