A 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 retains its activity in presence of SDS and urea. It is inactivated by diisopropyl fluorophosphates (DFP) and phenyl methane sulfonyl fluoride (PMSF).
Source:
Recombinant protein corresponding to Proteinase K, expressed in Tritirachium album.
Molecular Weight:
~28.9kD
Biological Activity:
>30units/mg
Unit Definition:
One unit is defined as the amount of enzyme that will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1mol tyrosine per min at 37 degrees C, pH 7.5 (color by Folin-Ciocalteu reagent).
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with 50mM Tris-HCl, 2mM calcium acetate, pH 8.0. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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