FabAct™ Proteinase K (recombinant), Molecular Grade (Solid)

A highly reactive serine protease that displays the ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids. The application of the molecular grade FabAct™ Proteinase K is similar to the Native Proteinase K and is used in the isolation or preparation of high molecular weight nucleic acids. However, FabAct™ Proteinase K is highly pure and has a higher specific activity and is more stable at room temperature as compared to native Proteinase K. It is stable and active over a wide pH range of 4-12. It can be used on any situation to digest native and denatured proteins. FabAct™ Proteinase K is also active with SDS, urea and EDTA and the most active temperature is 65°C. It is inactivated by diisopropyl fluorophosphates (DFP) and phenyl methane sulfonyl fluoride (PMSF).

N/A

29.3 kDa

Protease K, Endopeptidase K, Tritirachium alkaline proteinase

Protease K, Endopeptidase K, Tritirachium alkaline proteinase

5621

PROK

N/A

P06873

Yes

Tritirachium album limber gene, recombinant

≥99%

Native PAGE and SDS PAGE, N/A

N/A

1.07 kU/mg

N/A

N/A

N/A

One unit is defined as the amount of protease that cleaves the FITC-labeled casein substrate to yield an amount of fluorescence equivalent to 1.0 nmol of unquenched FITC per minute at 37°C, pH 8.0

4°C

Gel Pack

Lyophilized

Lyophilized with no additives

In 50 mM Tris-HCl (pH7.5), 3 mM CaCl2, 50% Glycerol

N/A

Centrifuge the vial prior to opening.

For Research Use Only! Not to be used in humans

Proteinase K s a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Engyodontium album (formerly Tritirachium album).Proteinase K is able to digest hair (keratin), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. This enzyme belongs to Peptidase family S8. The molecular weight of Proteinase K is 28,900 Daltons (28.9 kDa).

Recombinants or rec. proteins

recombinants