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Proteinase K, 1 g, 1 x 1 g

Proteinase K, 1 g, 1 x 1 g

SKU 7528.4
€ 718,93
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Proteinase K, 1 g, 1 x 1 g
Product Details
P-phrases: P210 P260 P280 P302+P352 P305+P351+P338 P308+P311
H-phrases: H225-H290-H302+H312+H332-H318-H336-H370
Hazard class: 3 (8) II
HS code: 35079090
Brand: Carl Roth
Proteinase K, lyophil., min. 30 mAnson U/mg, Storage temp. +4 °C, CAS No. [39450-01-6], EG-Nr. 254-457-8

Proteinase K (from Tritirachium album) is a non-specific protease of the serine protease family.
Proteinase K is used for the cleavage of proteins in nucleic acid preparations. It is mainly used in nucleic acid purification or for the removal of nucleases.
Proteinase K is active under a wide range of reaction conditions, including elevated temperatures and presence of SDS.


Gebruiksinstructies

Activity: (Haemoglobin, pH 7.5; 25 °C) 30 mAnson-U/mg
Foreign activity: RNAse and DNAse not detectable
Optimum temperature: +65 °C.
Activity at +65 °C is ca. 12 x higher than at +25 °C. Over +65 °C, inactivation due to denaturation.
Activators: Denaturating agents like SDS (0,5-1 %), urea.
Inhibitors: Inhibition with Hg2+-ions, DFP, PMSF and phenol. Not inhibited by EDTA, sulfhydryl reagents and trypsin or chymotryps ininhibitors.
Stability: pH 4.0-12.5. pH optimum: 8,0.
Also stable even when denaturing agents, e.g. SDS and urea are present.
Stabilisers: Ca2+-ions (1-5 mM) prevent autolysis.



Proteinase K ≥30 mAnson U/mg, lyophilized

A non-specific endopeptidase with strong proteolytic activity for degrading proteins in biological samples. A quality product for molecular biology with a broad scope of application.


Gebruiksinstructies

Working solution: 50 µg/ml
Reaction buffer: 50 mM Tris-HCl; pH 7.5; 5 mM CaCl2; 0.5 % SDS



Enzyme: a neoclassical, Greek artificial word ενζυμου, énzymon, derived from εν-, en- (in-) and ζυμη, zýmé (yeast, sourdough, archaic)
Ferments: comes from the Latin fermentum (ferments, sourdough)

There are six classes in which all enzymes are classified according to the particular reaction they catalyse:

• Oxidoreductases (catalyse redox reactions)

• Transferases (transfer functional groups among substrates)

• Hydrolases (cleave bonds via addition of water)

• Lyases/Synthases (cleave or synthesise complex products out of basic substrates without cleavage of ATP)

• Isomerases (transform chemical isomers)

• Ligases/Synthetases (cleave or synthesise complex products out of basic substrates via cleavage of ATP)


Enzyme: a neoclassical, Greek artificial word ενζυμου, énzymon, derived from εν-, en- (in-) and ζυμη, zýmé (yeast, sourdough, archaic)
Ferments: comes from the Latin fermentum (ferments, sourdough)

There are six classes in which all enzymes are classified according to the particular reaction they catalyse:

• Oxidoreductases (catalyse redox reactions)

• Transferases (transfer functional groups among substrates)

• Hydrolases (cleave bonds via addition of water)

• Lyases/Synthases (cleave or synthesise complex products out of basic substrates without cleavage of ATP)

• Isomerases (transform chemical isomers)

• Ligases/Synthetases (cleave or synthesise complex products out of basic substrates via cleavage of ATP)


Activity (Hemoglobin, 37 °C) ≥30 U/mg
DNases, RNases not detected
Endonucleases not detected
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