Proteinase
K
���������������������������������� Grade:High purity
grade, for Molecular Biology Cat#ES***1�
**0mg,�1g,�1kg����������������������������������� Storage Temperature�*0�C CAS# *********6 Purity:?*9% Specific activity:?*0 units/mg of
protein DNase� none
detected RNase� none
detected Endonuclease
(nickase)� none
detected
� Product Description Proteinase K is a stable serine protease with
broad substrate specificity. It degrades many proteins in the
native state even in the presence of detergents. Evidence from crystal and molecular structure
studies indicates the enzyme belongs to the subtilisin family with
an activesitecatalytic triad (Asp*9, His*9, Ser**4). 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.The mode and specificity of action has been
studied.Proteinase K is frequently used in molecular
biology applications to digest unwanted proteins, such
as nucleases from DNA or RNA preparations from microorganisms,
cultured cells, and plants.The enzyme is typically used at
*0�**0?g/ml in nucleic acid preparations at pH 7.5�8.0 and *7�C.
Incubation times vary from *0minutes to *8hours. Proteinase K is
usually denatured by subsequent phenol extractions, although it can
autodigest during long incubations. Proteinase K is active in 1% Triton X***0 and
fully active in 0.5% (w/v) SDS. SDS and urea will denature protein
substrates resulting in increased digestion rates.Proteinase K
itself is denatured much more slowly by these
agents.
� Unit Definition:One unit is defined as the amount of enzyme that
will liberate 1 �mol of tyrosine per minute at *7�C, pH
7.5.������
