C0888
Clostripain from Clostridium histolyticum
≥20 units/mg solid
Sinônimo(s):
Clostridiopeptidase B, Proteinase from Clostridium histolyticum
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About This Item
Produtos recomendados
Formulário
lyophilized powder
atividade específica
≥20 units/mg solid
peso molecular
15.4 kDa
41.7 kDa
Impurezas
salt, essentially free
temperatura de armazenamento
2-8°C
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Aplicação
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).
Ações bioquímicas/fisiológicas
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.
Embalagem
Bottomless glass bottle. Contents are inside inserted fused cone.
Qualidade
Purified, essentially salt-free
Definição da unidade
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 7.6 at 25 °C in the presence of 2.5 mM DTT.
Nota de análise
The enzyme must be activated for 2-3 hours before use by dissolving in 2.5 mM dithiothreitol containing 1.0 mM calcium acetate.
Inibidor
Nº do produto
Descrição
Preços
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órgãos-alvo
Respiratory system
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
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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