(Tritirachium album)

Catalog # Size
IB05400    100 mg

Physical Specifications
Activity (37°C)                 15-20 U/mg protein

Molecular Biology Specifications
DNase assay (Endo and Exo)        None Detected
RNase assay                 None Detected
Protease activity on Gel Substrate    Pass

Recommended Use
Proteinase K is a highly active proteolytic enzyme that is purified from the mold Tritirachium album. The enzyme has two binding sites for Ca++, which lie some distance from the active site and is not directly involved in the catalytic mechanism. Because the residual activity is usually sufficient to degrade proteins that commonly contaminate preparations of nucleic acids, digestion with Proteinase K is usually carried out in the presence of EDTA (to inhibit the action of Mg++ dependent nucleases). However, to digest highly resistant proteins such as keratin, it may be necessary to use a buffer containing 1 mMC2++ and no EDTA. At the end of the digestion, the Ca++ should be chelated by addition of EDTA (pH 8.0) to a final concentration of 2 mM before the nucleic acids are purified.

        Stock sol.    Concen.         Reaction         Temp.         Pretreatment
                in reaction    Buffer       

Proteinase    20 mg/ml    50 mg/ml    0.01 M Tris    37-56 oC        none required
        in H2O                 (pH 7.8)
                        0.005 M EDTA
                        0.5% SDS

Storage
Store dessicated at -20oC. Warm to room temperature before opening. Keep tightly sealed.

Warning
Sensitizer. Avoid contact with eyes, skin and clothing. Avoid breathing dust. Wash thoroughly with soap and water after handling. See Material Safety Data Sheet for additional information.