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P2922

Sigma-Aldrich

Endoproteinase Glu-C from Staphylococcus aureus V8

Type XVII-B, lyophilized powder, 500-1,000 units/mg solid

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)
MDL number:
MFCD01324998
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

type

Type XVII-B

Quality Level

200

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

Gene Information

Staphylococcus aureus subsp. aureus MW2 ... sspA(1003044)

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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.

Unit Definition

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.

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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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
From the Cover: Discovery of an unusual biosynthetic origin for circular proteins in legumes
Aaron G. Poth, Michelle L. Colgrave, et al.
Proceedings of the National Academy of Sciences of the USA, 108 (2011)
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
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