추천 제품
유형
Type XVII-B
Quality Level
양식
lyophilized powder
특이 활성도
500-1,000 units/mg solid
분자량
29 kDa
정제법
chromatography
배송 상태
wet ice
저장 온도
−20°C
유전자 정보
Staphylococcus aureus subsp. aureus MW2 ... sspA(1003044)
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관련 카테고리
애플리케이션
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.
생화학적/생리학적 작용
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.
단위 정의
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.
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
개인 보호 장비
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
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
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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
Judy Toews et al.
Analytica chimica acta, 676(1-2), 60-67 (2010-08-31)
Cross-linking of proteins in a complex requires the chemical modification of the proteins in order to form a covalent link. This can be achieved in vivo using formaldehyde as it is small and rapidly permeates the cell membrane. Previous model
문서
LC-UV-MS workflow details teriparatide peptide mapping, including enzymatic digestion, separation conditions, and QTOF mass spectrometer identification.
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