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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

Sinónimos:

V8 Protease

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100 UNITS
$59.100
500 UNITS
$151.000
2500 UNITS
$521.000

$59.100

Fecha estimada de envío17 de mayo de 2025

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100 UNITS
$59.100
500 UNITS
$151.000
2500 UNITS
$521.000

About This Item

Número de CAS:
66676-43-5
Comisión internacional de enzimas:
3.4.21.19 (BRENDA, IUBMB)
Número MDL:
MFCD01324998
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

$59.100

Fecha estimada de envío17 de mayo de 2025

tpo

Type XVII-B

Nivel de calidad

200

Formulario

lyophilized powder

actividad específica

500-1,000 units/mg solid

mol peso

29 kDa

purificado por

chromatography

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

Información sobre el gen

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

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Aplicación

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]

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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.

Pictogramas

Health hazard
GHS08

Palabra de señalización

Danger

Frases de peligro

H317,H334

Clasificaciones de peligro

Resp. Sens. 1 - Skin Sens. 1

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Equipo de protección personal

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

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Certificados de análisis (COA)

Lot/Batch Number
0000427946
0000427946
0000408423
0000420156
SLCM2238

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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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