EnzymoPure™, Native activity: ≥ 5.0 U/mg (BAEE) EnzymoPure™ for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Description
Clostripain also known as Clostridiopeptidase B or Endoproteinase Arg-C is a proteinase that cleaves peptide bonds on the carboxyl side of arginine. This protein is a heterodimer composed of a heavy and a light chain that are held together via strong noncovalent forces. As a proteolytic enzyme it can be used for isolation of various cell types by tissue dissociation.
Clostripain exists in two different forms, an oxidized, native condition and a reduced activated form that differ in enzymatic activity. The native clostripain can be activated with reducing agents (e.g. DTT, Cysteine) resulting in a higher activity of the enzyme.
Application
Clostripain NB is used in combination with Collagenase NB 1 and/or Neutral Protease NB, suitable for cell isolation from various tissue types.
Specifications
Contains chromatographically highly purified clostripain.
Clostripain, native state activity: ≥ 5.0 U/mg (BAEE)
Clostripain, activated activity: ≥ 50.0 U/mg (BAEE)
Clostripain activity, native state, per vial: ≥ 200 U/vial (BAEE)
Clostripain activity, activated, per vial: status
EC 3.4.24.3 • Mr ca. 59 000 • CAS [9028-00-6]
References and Definitions
Unit definition:
Clostripain, native state (BAEE assay): 1 Unit catalyzes the cleavage of 1 µmol Nα-Benzoyl-L-arginine ethyl ester per minute at 25 °C, pH 7.8.
Clostripain, activated (BAEE assay): 1 Unit catalyzes the cleavage of 1 µmol Nα-Benzoyl-L-arginine ethyl ester per minute at 25 °C, pH 7.8. The enzyme is activated with 2.5 mM DTT.
References
1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-3091
2. Kula et al. (1976) Biochem. Biophys. Res. Commun. 69, 389-396
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