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COLLDISP-RO

Roche

Collagenase/Dispase®

lyophilized, non-sterile, optimum pH 7.0-8.0

Synonym(s):

collagenase

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About This Item

UNSPSC Code:
12352204

biological source

enzyme from Bacillus polymyxa ( Dispase )
enzyme from bacterial ( Collagenase from Vibrio alginolyticus)

Quality Level

100

sterility

non-sterile

form

lyophilized

collagenase activity

>0.1 U/mg lyophilizate, 25 °C (4-phenyl-azobenzyl-oxycarbonyl-Pro-Leu-Gly-Pro-D-Arg as substrate)

specific activity

>0.8 U/mg lyophilizate, pH 7.5, 37 °C (casein as substrate, Dispase)

packaging

pkg of 100 mg (10269638001)
pkg of 500 mg (11097113001)

manufacturer/tradename

Roche

concentration

1 mg/mL (Collagenase: 0.1U/mL, Dispase: 0.8U/mL)

technique(s)

tissue processing: suitable

color

light yellow to brown

optimum pH

7.0-8.0

solubility

water: soluble

UniProt accession no.

P43154

application(s)

life science and biopharma
sample preparation

foreign activity

proteolytic activities <0.1 U/mg (hemoglobin as the substrate)

storage temp.

2-8°C

Related Categories

General description

Dispase is a neutral, rapid-acting, gentle protease that separates intact epidermis from dermis. It also separates cultured intact epithelial cells from the substratum. It cleaves the basement membrane zone and leaves the epithelial cells intact. Collagenase is a protease which cleaves the triple-helical protein called collagen. There are three types of tissue collagenases, and these belong to the matrix metalloproteinases (MMP) family. Collagenase obtained from Clostridium histolyticum has a very strong activity, as it digests collagen from both ends, at temperatures as low as 4-10 °C.

Specificity

Collagenase degrades native collagen. Dispase® is a nonspecific protease.

Application

Collagenase/Dispase® is used for the preparation of cells from a wide variety of different tissues and organs.

Components

EC 3.4.24.4 & 3.4.24.3

Unit Definition

One unit is the enzyme activity, which liberates under assay conditions within 1 minute Folin-positive amino acids and peptides corresponding to 1 μmol tyrosine.

Preparation Note

Activator: Ca2+

Working concentration: Approximately 1mg/mL (Collagenase: 0.1U/mL, Dispase: 0.8U/mL)

Enzyme activity:
Collagenase: 0.1 Wünsch U/mg lyophilizate (+25°C, 4-phenyl-azobenzyl-oxycarbonyl-Pro-Leu-Gly-Pro-D-Arg as the substrate)
Dispase®: 0.8 Wünsch U/mg lyophilizate (+37°C, casein as substrate, pH 7.5)
Contaminating proteolytic activities: <0.1U/mg lyophilizate (hemoglobin as the substrate)

Working solution: Preparation of working solution Dissolve enzyme in water to a final concentration of 100mg/mL. Dilute with PBS (Ca2+/Mg2+-free) to a final concentration of 1mg/mL and filter through a sterile 0.2μm membrane filter.
Enzyme concentration of the sterile solution: Collagenase, 0.1U/mL PBS; Dispase®, 0.8U/mL PBS.

Inhibitors:
Collagenase inhibitors: EDTA, EGTA
Collagenase/Dispase is not inhibited by serum.

Storage conditions (working solution): -15 to -25°C
The reconstituted solution is stable at -15 to -25°C.
Note: Store in appropriate aliquots and avoid repeated freezing and thawing!

Reconstitution

Reconstitution in water (100mg/mL). Further dilution with PBS (phosphate buffered saline) (Ca2+/Mg2+-free).

Storage and Stability

Store dry

Other Notes

Collagenase from Vibrio alginolyticus, Dispase® from Bacillus polymyxa
For life science research only. Not for use in diagnostic procedures.

Legal Information

Dispase is a registered trademark of Godo Shusei Co., Ltd.

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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