C0888
梭菌蛋白酶 来源于溶组织梭菌
≥20 units/mg solid
别名:
梭菌肽酶B, 蛋白酶 来源于溶组织梭菌
产品名称
梭菌蛋白酶 来源于溶组织梭菌, ≥20 units/mg solid
form
lyophilized powder
specific activity
≥20 units/mg solid
mol wt
15.4 kDa
41.7 kDa
impurities
salt, essentially free
storage temp.
2-8°C
Quality Level
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Analysis Note
本品在使用前，要先溶于含1.0 mM乙酸钙的2.5 mM二硫苏糖醇中活化2-3小时。
纯化制品，基本上不含盐
Application
梭菌蛋白酶（源于溶组织梭菌）已用作灌注液的蛋白水解酶，检测其对管中血细胞比容(tube hematocrit)的影响。还用于T4噬菌体(RB69 gp43)DNA聚合酶(gp43)的限制性分解。
Biochem/physiol Actions
梭菌蛋白酶，来自溶组织梭菌，由两条分子量各为41.7 kDa和15.4 kDa的肽链组成。梭菌蛋白酶对Arg-Xaa肽键具有高限制性的底物特异性。因此，梭菌蛋白酶可服务于蛋白测序。据研究，它也可作为催化剂，用于缩合含Arg-Pro肽键的重要药物肽。
Other Notes
25 °C、pH 7.6，在2.5 mM DTT存在条件下，一个单位每分钟水解1.0μmole BAEE。
Packaging
无底玻璃瓶。内含物装在锥底内插管中。
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
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
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
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
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
V Witte et al.
Microbiology (Reading, England), 140 ( Pt 5), 1175-1182 (1994-05-01)
Clostripain-specific antibodies were used to analyse the maturation of clostripain prepro-enzyme and core protein heterologously synthesized in Escherichia coli and Bacillus subtilis. Core protein purified from E. coli cells harbouring plasmid pHM3-23 underwent calcium-dependent, self-triggered maturation. Concomitantly, the inactive form
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