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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

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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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)
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)
all-D-Polypeptides: novel targets for semisynthesis.
Nicole Wehofsky et al.
Angewandte Chemie (International ed. in English), 42(6), 677-679 (2003-02-08)
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
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