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Roche

Collagenase P

from Clostridium histolyticum

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Enzyme Commission number:
3.4.24.3 (BRENDA, IUBMB)

biological source

Clostridium histolyticum

Quality Level

100

sterility

non-sterile

form

lyophilized

collagenase activity

>1.5 U/mg (Lyophilizate, Collagenase activity)

packaging

pkg of 1 g (11249002001)
pkg of 100 mg (11213857001)
pkg of 2.5 g (11213873001)
pkg of 500 mg (11213865001)

manufacturer/tradename

Roche

concentration

0.5-2.5 mg/mL

technique(s)

tissue processing: suitable

color

light brown to brown

solubility

water: soluble

NCBI accession no.

WP_138210331

application(s)

life science and biopharma

foreign activity

Clostripain 24.099 U/mg
Protease 4.4 U/mg (Proteases)
Trypsin 53.428 U/mg (with BAEE)

storage temp.

2-8°C

Related Categories

General description

Collagenase P is an enzyme mixture prepared from the extracellular culture filtrate of a special Clostridium histolyticum strain.Collagenase P is a research biochemical, not manufactured under the US good manufacturing practices (GMP) regulations.
Note: Collagenase P is a non-sterile preparation of the culture supernatant of Clostridium histolyticum. It is neither designed nor intended for isolation of pancreatic islets for transplantation into humans and must not be used for such purposes.

Specificity

Enzyme activity:
Collagenase activity: >1.5U/mg (according to Wünsch) (+25°C, 4-phenyl-azobenzyl-oxycarbonyl-Pro-Leu-Gly-Pro-D-Arg as the substrate)
Contaminating enzyme activities: trypsin, clostripain, and total proteolytic activity
Collagenase P has a very high collagenase activity (>1.5U/mg), and is function tested for the isolation of mouse pancreatic islets.
Specificity: Collagenase degrades native collagen. Clostripain, trypsin-like enzymes, and neutral proteases degrade other proteins as well.

Application

Collagenase from C. histolyticum is used for the dissociation of tissues for the establishment of primary cell cultures. Because of its high collagenase activity Collagenase P is particularly suitable for the isolation of pancreatic islets from mouse and rat (function tested). The preparation is also suitable for the isolation of adipocytes from epididymal fat pads of rats.

Features and Benefits

Contents:
Lyophilizate, nonsterile

Preparation Note

Activator: Ca2+
Inhibitors:
Collagenase inhibitors: EDTA, EGTA, Cys, His, DTT, 2-mercaptoethanol
Collagenase is not inhibited by serum.
Clostripain inhibitors: TLCK
Trypsin inhibitors: aprotinin, trypsin inhibitor (egg white, soybean)
Working concentration: 0.5 to 2.5mg/ml
0.5 to 1.5mg/ml for the isolation of pancreatic islets from mouse and rat pancreas.
Approximately 2mg/ml for the isolation of adipocytes.
Storage conditions (working solution): -15 to -25°C
The reconstituted solution is stable at -15 to -25°C. Prepare appropriate aliquots and avoid repeated freezing and thawing.

Reconstitution

Reconstitution in any balanced salt solution (e.g., HBSS)

Storage and Stability

Store dry

Other Notes

For life science research only. Not for use in diagnostic procedures.

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315 - H319 - H334 - H335

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 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash

Regulatory Information

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T-cadherin (Cdh13) in association with pancreatic ?-cell granules contributes to second phase insulin secretion.
Tyrberg B
Islets, 3(6), 327-337 (2011)
Luigi Racioppi et al.
The Journal of biological chemistry, 287(14), 11579-11591 (2012-02-16)
Calcium/calmodulin-dependent kinase kinase 2 (CaMKK2) plays a key role in regulating food intake and energy expenditure at least in part by its actions in hypothalamic neurons. Previously, we showed that loss of CaMKK2 protected mice from high-fat diet (HFD)-induced obesity
Fumin Lin et al.
Endocrinology, 152(10), 3668-3679 (2011-08-25)
When fed a standard chow diet, CaMKK2 null mice have increased adiposity and larger adipocytes than do wild-type mice, whereas energy balance is unchanged. Here, we show that Ca(2+)/calmodulin-dependent protein kinase kinase 2 (CaMKK2) is expressed in preadipocytes, where it

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