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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

Sinonimo/i:

V8 Protease

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100 UNITS
CHF 79.60
500 UNITS
CHF 243.00
2500 UNITS
CHF 792.00

CHF 79.60

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Cambia visualizzazione
100 UNITS
CHF 79.60
500 UNITS
CHF 243.00
2500 UNITS
CHF 792.00

About This Item

Numero CAS:
66676-43-5
Classificazione EC (Enzyme Commission):
3.4.21.19 (BRENDA, IUBMB)
Numero MDL:
MFCD01324998
Codice UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

CHF 79.60

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Tipo

Type XVII-B

Livello qualitativo

200

Stato

lyophilized powder

Attività specifica

500-1,000 units/mg solid

PM

29 kDa

Purificato mediante

chromatography

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

Informazioni sul gene

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

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Categorie correlate

Applicazioni

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[1].
Endoproteinase Glu-C from Staphylococcus aureus V8 has been used to digest reduced and alkylated cyclotides to produce linearized fragments.[2]
It is used for selective cleavage of proteins for amino acid sequence determination[3] or peptide mapping.[4]

Azioni biochim/fisiol

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.

Definizione di unità

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.[5] One unit is equivalent to ~0.004 casein digestion unit.

Pittogrammi

Health hazard
GHS08

Avvertenze

Danger

Indicazioni di pericolo

H317,H334

Classi di pericolo

Resp. Sens. 1 - Skin Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Dispositivi di protezione individuale

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

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Certificati d'analisi (COA)

Lot/Batch Number
0000408423
0000408423
0000427946
0000427946
0000420156

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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
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
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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