C0888
Clostripain from Clostridium histolyticum
≥20 units/mg solid
Synonym(s):
Clostridiopeptidase B, Proteinase from Clostridium histolyticum
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About This Item
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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
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Application
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 Actions
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.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Quality
Purified, essentially salt-free
Unit Definition
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.
Analysis Note
The enzyme must be activated for 2-3 hours before use by dissolving in 2.5 mM dithiothreitol containing 1.0 mM calcium acetate.
inhibitor
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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J S Nishimura et al.
The Journal of biological chemistry, 268(18), 13717-13722 (1993-06-25)
Mutant forms of Escherichia coli succinyl-CoA synthetase, W76F (Trp beta 76 replaced by Phe) (Nishimura, J. S., Mann, C. J., Ybarra, J., Mitchell, T., and Horowitz, P. M. (1990) Biochemistry 29, 862-865), and W43,76,248F (all three Trp replaced by Phe)
The activity of Clostridium histolyticum proteinase on synthetic substrates.
J D OLGE et al.
Archives of biochemistry and biophysics, 42(2), 327-336 (1953-02-01)
Barney Yoo et al.
Journal of the American Chemical Society, 127(49), 17132-17133 (2005-12-08)
We demonstrate that proteases can catalyze the ligation of peptidomimetic oligomers. The enzyme clostripain was used to facilitate the native ligation of N-substituted glycine oligomers, or peptoids. In addition to mediating the efficient condensation of two peptoid fragments, iterative ligation
Nicholas J Carruthers et al.
European journal of pharmacology, 555(2-3), 106-114 (2006-12-05)
Calcineurin, the Ca2+/calmodulin-dependant serine/threonine phosphatase is the target for the immunosuppressant drugs FK506 and cyclosporine-A. These established calcineurin inhibitors each require an immunophilin protein cofactor. Gossypol, a polyphenol produced by the cotton plant, inhibits calcineurin (IC50=15 microM), in a noncompetitive
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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