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Merck

C0888

Sigma-Aldrich

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

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About This Item

CAS号:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352204
NACRES:
NA.54

形狀

lyophilized powder

品質等級

比活性

≥20 units/mg solid

分子量

15.4 kDa
41.7 kDa

雜質

salt, essentially free

儲存溫度

2-8°C

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相关类别

應用

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。

生化/生理作用

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。

包裝

无底玻璃瓶。内含物装在锥底内插管中。

品質

纯化制品,基本上不含盐

單位定義

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。

分析報告

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。

抑制劑

产品编号
说明
价格

象形圖

Health hazardExclamation mark

訊號詞

Danger

危險分類

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

標靶器官

Respiratory system

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

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
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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