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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

Synonyme(s) :

V8 Protease

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About This Item

Numéro CAS:
66676-43-5
Numéro de classification (Commission des enzymes):
3.4.21.19 (BRENDA, IUBMB)
Numéro MDL:
MFCD01324998
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Type

Type XVII-B

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

500-1,000 units/mg solid

Poids mol.

29 kDa

Produit purifié par

chromatography

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H317,H334

Classification des risques

Resp. Sens. 1 - Skin Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Équipement de protection individuelle

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

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
Yurgis Av Yomantas et al.
Microbial cell factories, 10, 64-64 (2011-08-09)
Plasmid-less, engineered Bacillus strains have several advantages over plasmid-carrier variants. Specifically, their stability and potential ecological safety make them of use in industrial applications. As a rule, however, it is necessary to incorporate many copies of a key gene into
Hélio Nitta Matsuura
Methods in molecular biology (Clifton, N.J.), 2469, 165-181 (2022-05-05)
Cyclotides are small circular peptides carrying an array of interesting biological activities and also showing interesting features for storage and bioavailability. Here, an optimized method to isolate cyclotides from two species of Psychotria, P. brachyceras and P. leiocarpa, that can
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)
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