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C0888

Clostripain from Clostridium histolyticum

≥20 units/mg solid

Sinónimos:

Clostridiopeptidase B, Proteinase from Clostridium histolyticum

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Tamaño de envaseSKUDisponibilidadPrecio
250 units

Disponible para enviar HOYdesdeMILWAUKEE

$937.00

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Número CAS:
9028-00-6
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-822-2
MDL number:
MFCD00130814
Número CE:
3.4.22.8 (BRENDA, IUBMB)
Specific activity:
≥20 units/mg solid

$937.00

Disponible para enviar HOYDetalles

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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

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).[1]

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.[2]

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

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.
Purified, essentially salt-free

Other Notes

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.

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Este artículo
C5894C1639C2014
Clostripain from Clostridium histolyticum ≥20 units/mg solid

Sigma-Aldrich

C0888

Clostripain from Clostridium histolyticum

Collagenase from Clostridium histolyticum non-sterile; 0.2 μm filtered, Type IA-S, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid

Sigma-Aldrich

C5894

Collagenase from Clostridium histolyticum

Collagenase from Clostridium histolyticum 0.2 μm filtered, for general use, Type I-S, 0.2-1.0 FALGPA units/mg solid, ≥125 CDU/mg solid

Sigma-Aldrich

C1639

Collagenase from Clostridium histolyticum

Collagenase from Clostridium histolyticum 0.2 μm filtered, Type V-S, ≥1 FALGPA units/mg solid, ≥125 CDU/mg solid

Sigma-Aldrich

C2014

Collagenase from Clostridium histolyticum

specific activity

≥20 units/mg solid

specific activity

≥125 CDU/mg solid, 0.5-5.0 FALGPA units/mg solid

specific activity

≥125 CDU/mg solid, 0.2-1.0 FALGPA units/mg solid

specific activity

≥1 FALGPA units/mg solid, ≥125 CDU/mg solid

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

15.4 kDa, 41.7 kDa

mol wt

68-130 kDa

mol wt

68-130 kDa

mol wt

68-125 kDa

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

impurities

salt, essentially free

impurities

-

impurities

-

impurities

-

Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

200

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

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
BCCP6526
BCCK2455
BCCJ2943
BCCH9520
BCCH4761

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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
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
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SKUGTIN
C0888-250UN04061833452455

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