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C0888
Clostripain aus Clostridium histolyticum
≥20 units/mg solid
Synonym(e):
Clostridiopeptidase B, Proteinase
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About This Item
Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
≥20 units/mg solid
Mol-Gew.
15.4 kDa
41.7 kDa
Verunreinigungen
salt, essentially free
Lagertemp.
2-8°C
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Anwendung
Clostripain from Clostridium histolyticum has been used as a proteolytic enzyme in perfusate to detect its effect on tube hematocrit. It has also been used in limited proteolysis of DNA polymerase (gp43) of phage T4 (RB69 gp43).
Biochem./physiol. Wirkung
Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substrate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds.
Verpackung
Bottomless glass bottle. Contents are inside inserted fused cone.
Qualität
Gereinigt, weitgehend Salz-frei
Einheitendefinition
1 U hydrolysiert 1.0 μmol BAEE pro Minute bei pH 7.6 und 25 °C in Anwesenheit von 2.5 mM DTT.
Hinweis zur Analyse
Das Enzym muss 2-3 Stunden vor Gebrauch aktiviert werden, indem es in 2.5 mM Dithiothreitol mit 1.0 mM Calciumacetat gelöst wird.
Inhibitor
Produkt-Nr.
Beschreibung
Preisangaben
Signalwort
Danger
H-Sätze
Gefahreneinstufungen
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Zielorgane
Respiratory system
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Chang-Kyu Kim et al.
Journal of biotechnology, 131(3), 346-352 (2007-09-05)
In this study, the clostripain gene was modified and its signal sequence was replaced with that of penicillin G acylase (PGA). The core clostripain protein fused to the PGA signal peptide was also prepared. With regard to the expression of
Ozlem Doğan Ekici et al.
Journal of medicinal chemistry, 47(8), 1889-1892 (2004-04-02)
Aza-peptide Michael acceptors are a new class of irreversible inhibitors that are highly potent and specific for clan CD cysteine proteases. The aza-Asp derivatives were specific for caspases, while aza-Asn derivatives were effective legumain inhibitors. Aza-Lys and aza-Orn derivatives were
Nikolaos E Labrou et al.
European journal of biochemistry, 271(5), 983-992 (2004-03-11)
In this study we investigate the active-site structure and the catalytic mechanism of clostripain by using a combination of three separate techniques: affinity labelling, site-directed mutagenesis and molecular modelling. A benzamidinyl-diazo dichlorotriazine dye (BDD) was shown to act as an
Antibacterial activity of casein-derived peptides isolated from rabbit (Oryctolagus cuniculus) milk.
Maria Baranyi et al.
The Journal of dairy research, 70(2), 189-197 (2003-06-13)
Acid-precipitated rabbit 'whole casein' was digested by trypsin, chymotrypsin, pepsin, and clostripain to screen for possible peptides with antibacterial properties. The peptide fragments were separated by reversed-phase chromatography. The collected fractions were pooled and their antibacterial properties tested against Escherichia
Synthesis of neo-peptidoglycans: an unexpected activity of proteases.
Nicole Wehofsky et al.
Angewandte Chemie (International ed. in English), 41(15), 2735-2738 (2002-08-31)
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