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53702

Millipore

Pronase® Protease, Streptomyces griseus

Synonym(s):

Pronase® powder

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.54

form

lyophilized

Quality Level

specific activity

≥45,000 proteolytic units/g dry wt

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)

solubility

water: 10 mg/mL

shipped in

ambient

storage temp.

2-8°C

General description

A non-specific protease liquefies mucins and digests proteins to free amino acids. Can be used to isolate living chondrocytes. Most active at neutral pH, but it is stable over a wide pH and temperature range. Has an optimal pH of 7.5. Note: 1 KU = 1000 units.
A non-specific protease liquefies mucins and digests proteins to free amino acids. Can be used to isolate living chondrocytes. Most active at neutral pH, but stable over wide range of pH and temperature. Note: 1KU = 1000 units.
Note: 1 KU = 1000 units.

Warning

Toxicity: Harmful (C)

Unit Definition

One unit is defined as the amount of enzyme that will liberate a digestion product equivalent to 25 µg of tyrosine per min at 40°C, pH 7.5.

Physical form

Lyophilized from a solution containing calcium acetate as a stabilizer.

Reconstitution

Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for 24 h at 4°C.

Other Notes

Narahashi, Y., et al. 1968. J. Biochem. 64, 427.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
PRONASE is a registered trademark of Merck KGaA, Darmstadt, Germany

pictograms

Health hazardExclamation mark

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 2


Certificates of Analysis (COA)

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W N Ross et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 4(3), 659-672 (1984-03-01)
Optical techniques using voltage-sensitive dyes were used to record electrical events simultaneously from many positions on certain neurons of the barnacle supraesophageal ganglion. By signal-averaging, recordings with good signal-to-noise ratios and time resolution were obtained from fine dendritic processes as
T E Davis et al.
Infection and immunity, 15(3), 978-987 (1977-03-01)
Enzymes capable of hydrolyzing cell walls of Blastomyces dermatitidis and chemotypes I and II of Histoplasma capsulatum were prepared in the laboratory or obtained from commercial sources. They included chitinases, beta-1,3-glucanases, beta-1,6-glucanase, and Pronase. Monosaccharides and disaccharides of glucose released
Saurabh Dahiya et al.
Human molecular genetics, 20(22), 4345-4359 (2011-08-19)
Matrix metalloproteinases (MMPs) are a group of extracellular proteases involved in tissue remodeling in several physiological and pathophysiological conditions. While increased expression of MMPs (especially MMP-9) has been observed in skeletal muscle in numerous conditions, their physiological significance remains less-well
M Tsacopoulos et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 17(7), 2383-2390 (1997-04-01)
Glial cells transform glucose to a fuel substrate taken up and used by neurons. In the honeybee retina, photoreceptor neurons consume both alanine supplied by glial cells and exogenous proline. Ammonium (NH4+) and glutamate, produced and released in a stimulus-dependent
S Kästner et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 48(8), 1079-1096 (2000-07-18)
Satellite cells are the myogenic precursors in postnatal muscle and are situated beneath the myofiber basement membrane. We previously showed that fibroblast growth factor 2 (FGF2, basic FGF) stimulates a greater number of satellite cells to enter the cell cycle

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