This endoproteinase is not sterile and has not been tested for suitability in cell culture. It is recommended for use in protein sequencing assays.
P6181
Glu-C Protease
Cleaves at glutamic acid residues, suitable for Mass Spectrometry, from Staphylococcus aureus V8
Synonym(s):
V8 Protease
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50 μG
$263.00
$263.00
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
200-350-6
MDL number:
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Product Name
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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Related Categories
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This Item | P2922 | 324713 | 10791156001 |
|---|---|---|---|
| grade Proteomics Grade | grade - | grade Proteomics Grade | grade - |
| suitability suitable for protein sequencing | suitability - | suitability - | suitability - |
| form lyophilized powder | form lyophilized powder | form lyophilized | form lyophilized (salt-free) |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. - |
| Quality Level 200 | Quality Level 200 | Quality Level 100 | Quality Level - |
| analyte chemical class(es) amino acids | analyte chemical class(es) - | analyte chemical class(es) - | analyte chemical class(es) - |
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.[1]
- the enzymatic cleavage of native VSTx-3 (voltage sensor toxin 3) peptide for its sequence determination.[2]
- limited proteolysis of recombinant purified PimA (phosphatidylinositol mannosyltransferase).[3]
- the digestion of glycosylated hemoglobin for isotope dilution liquid chromatography-tandem mass spectrometry analysis.[4]
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.[5] 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.[6] Glu-C is reported to be active in the presence of 0.2% SDS (sodium dodecyl sulfate) and in 4.0M urea.[7]
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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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
Protocols
An optimized LC-MS/MS based workflow for low artifact tryptic digestion and peptide mapping of monoclonal antibody, adalimumab (Humira) using filter assisted sample preparation (FASP).
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Instructions
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Hi, is this enzyme sterile and suitable for cell culture? Thank you.
1 answer-
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Hi, I was just wondering you can give me the amino acid sequence for this protein. I can't find it on the page.
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The product does not need to be sequenced to get released. Unfortunately there is no in-house information about product sequence.
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