P2922
Endoproteinase Glu-C from Staphylococcus aureus V8
Type XVII-B, lyophilized powder, 500-1,000 units/mg solid
Synonyme(s) :
V8 Protease
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
MDL number:
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Endoproteinase Glu-C from Staphylococcus aureus V8, Type XVII-B, lyophilized powder, 500-1,000 units/mg solid
type
Type XVII-B
form
lyophilized powder
specific activity
500-1,000 units/mg solid
mol wt
29 kDa
purified by
chromatography
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
Staphylococcus aureus subsp. aureus MW2 ... sspA(1003044)
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Catégories apparentées
Application
Endoproteinase Glu-C from Staphylococcus aureus strain V8 is a serine protease used for selective cleavage of proteins for amino acid sequence determination or peptide mapping . Product P2922 has been used to linearize cyclic peptides in C. ternatea leaf extract.
Endoproteinase Glu-C from Staphylococcus aureus V8 has been used to digest reduced and alkylated cyclotides to produce linearized fragments.
It is used for selective cleavage of proteins for amino acid sequence determination or peptide mapping.
Biochem/physiol Actions
Staphylococcus strain V8 protease specifically cleaves peptide bonds on the carboxyl side of aspartic and glutamic acid residues when used in phosphate buffer. When used in ammonium bicarbonate buffer or ammonium acetate buffer cleavage is restricted to the carboxyl side of glutamic acid residues only. The enzyme exhibits maximal activity from pH 4.0 to 7.8. If hemoglobin is used as the substrate, maximal activity is at pH 4.0. The maximal activity is at pH of 7.8 when casein is the substrate.
Other Notes
One unit will hydrolyze 1 μmole of N-t-Boc-L-glutamic acid α-phenyl ester per min at pH 7.8 at 37 °C. One unit is equivalent to ~0.004 casein digestion unit.
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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Shanshan Liu et al.
Amino acids, 48(4), 1059-1067 (2016-01-11)
Common yet often overlooked, deamidation of peptidyl asparagine (Asn or N) generates aspartic acid (Asp or D) or isoaspartic acid (isoAsp or isoD). Being a spontaneous, non-enzymatic protein post-translational modification, deamidation artifact can be easily introduced during sample preparation, especially
Andrew Michael Frey et al.
Cell reports, 35(1), 108930-108930 (2021-04-08)
Staphylococcus aureus possesses ten extracellular proteases with mostly unknown targets in the human proteome. To assist with bacterial protease target discovery, we have applied and compared two N-terminomics methods to investigate cleavage of human serum proteins by S. aureus V8 protease
Jason M Gilmore et al.
Analytical and bioanalytical chemistry, 402(2), 711-720 (2011-10-18)
Protein phosphorylation is a reversible post-translational modification known to regulate protein function, subcellular localization, complex formation, and protein degradation. Detailed phosphoproteomic information is critical to kinomic studies of signal transduction and for elucidation of cancer biomarkers, such as in non-small-cell
Aaron G Poth et al.
The Journal of biological chemistry, 287(32), 27033-27046 (2012-06-16)
Cyclotides are a large family of plant peptides that are structurally defined by their cyclic backbone and a trifecta of disulfide bonds, collectively known as the cyclic cystine knot (CCK) motif. Structurally similar cyclotides have been isolated from plants within
Chung-Ping Leon Wan et al.
Biochimica et biophysica acta, 1808(3), 606-613 (2010-11-30)
Apolipoprotein mediated formation of nanodisks was studied in detail using apolipophorin III (apoLp-III), thereby providing insight in apolipoprotein-lipid binding interactions. The spontaneous solubilization of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles occured only in a very narrow temperature range at the gel-liquid-crystalline phase transition
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