C0888
Clostripain from Clostridium histolyticum
≥20 units/mg solid
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form
lyophilized powder
Quality Level
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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Andrew K Ottens et al.
Journal of neurochemistry, 104(5), 1404-1414 (2007-11-27)
Neurotrauma, as in the case of traumatic brain injury, promotes protease over-activation characterized by the select fragmentation of brain proteins. The resulting polypeptides are indicators of biochemical processes, which can be used to study post-injury dynamics and may also be
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
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
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
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)
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