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

Catalog number
9212-10G
Name
FabAct™ Proteinase K (recombinant), Molecular Grade (Solid)
Size
10 g
Price
4726.00 EUR
Supplier

Details

Background
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).
Concentration
N/A
Molecular weight
29.3 kDa
Synonym
Protease K, Endopeptidase K, Tritirachium alkaline proteinase
Other name
Protease K, Endopeptidase K, Tritirachium alkaline proteinase
NCBI gene number
5621
NCBI gene
PROK
Gene source
N/A
NCBI number
P06873
Recombinant
Yes
Source
Tritirachium album limber gene, recombinant
Purification
≥99%
Tested applications
Native PAGE and SDS PAGE, N/A
Level of endotoxin
N/A
Tested activity
1.07 kU/mg
Biological activity
N/A
Reesults
N/A
Binding ability
N/A
Unit
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
Storage condition
4°C
Shipping under
Gel Pack
Physical appearance
Lyophilized
Physical properties
Lyophilized with no additives
How to reconstitute
In 50 mM Tris-HCl (pH7.5), 3 mM CaCl2, 50% Glycerol
Aa sequence
N/A
Before use
Centrifuge the vial prior to opening.
Notes
For Research Use Only! Not to be used in humans
Gene
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).
Additional source
Recombinants or rec. proteins
Group
recombinants