from Tritirachium album
Endopeptidase K
Cat. No. | Amount | Price (EUR) | Buy / Note |
---|---|---|---|
EN-178S | 2 x 1 ml | 72,00 | Add to Basket/Quote Add to Notepad |
EN-178L | 10 x 1 ml | 287,70 | Add to Basket/Quote Add to Notepad |
For general laboratory use.
Unit Definition: One unit of Proteinase K hydrolyzes urea-denatured hemoglobin producing color equivalent of 1 μmol tyrosine per 1 min at 37°C and pH 7.5 (Folin & Ciocalteu’s method), 1 U = 1 mAnsonU.
Shipping: shipped on gel packs
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 28.9 kDa
CAS#: 39450-01-6
EC number: 254-457-8
Purity: free of RNases, DNases and Exonucleases
Form: Proteinase K solution in 10 mM Tris-HCl, 1 mM Ca(H3C2O2)2, 10 % (v/v) Glycerol, pH 7.8 (22°C)
Concentration: 20 mg/ml
Activity:
> 600 mAnsonU/ml
Applications:
Digestion of proteins during DNA and RNA preparation.
Description:
Proteinase K is a serine protease that exhibits a very broad cleavage specificity. The Protein with a molecular weight of 28.9 kDa cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids. Proteinse K is not inactivated by metal chelating reagents such as EDTA or detergents such as SDS and is active over a wide range of pH (4 - 12.5).
Proteinase K is a highly active and stable protease with low cutting specificity. The enzyme belongs to the group of subtilisine-related serine proteases and is strongly inhibited by PMSF.
In presence of 0.5 - 1 % SDS Proteinase K inactivates DNases and RNases in eucaryotic and microbiological cell cultures. The use of Proteinase K during lysis of the cells allows the isolation of intact highly-molecular nucleic acids.
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