P2922
Endoproteinase Glu-C from Staphylococcus aureus V8
Type XVII-B, lyophilized powder, 500-1,000 units/mg solid
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Synonym(s):
V8 Protease
CAS Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Recommended Products
type
Type XVII-B
Quality Level
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
WGK
WGK 3
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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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
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)
Articles
LC-UV-MS workflow details teriparatide peptide mapping, including enzymatic digestion, separation conditions, and QTOF mass spectrometer identification.
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