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C0888

Sigma-Aldrich

Clostripain from Clostridium histolyticum

≥20 units/mg solid

Synonym(s):

Clostridiopeptidase B, Proteinase from Clostridium histolyticum

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About This Item

CAS Number:
9028-00-6
Enzyme Commission number:
3.4.22.8 (BRENDA, IUBMB)
EC Number:
232-822-2
MDL number:
MFCD00130814
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

100

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

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

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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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
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
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
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
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)
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