Proteinase K

Introduction

Proteinase K exhibits broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. Proteinase K is isolated from a fungus, Beauveria brongniartii which is able to grow on keratin. 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. Proteinase K is a stable and highly reactive serine protease. It is stable in a broad range of environments: pH (4 to 12.5), buffer salts, detergents (0.1-0.5% SDS) and temperature (0 to 75 ℃). Proteinase K is commonly used in molecular biology to digest protein and remove contamination from preparations of nucleic acid. It is also used in leather industry (leather softening, leather refinement, leather depilation and silk degumming), food industry (meat tenderization and wine clarification) and detergent industry. It is highly suited to this application since the enzyme is active in the presence of chemicals that denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is used for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, since it very effectively inactivates DNases and RNases.

Physical Properties:

Appearance (Color): White to Off White

Appearance (Form): Powder

Product name: Proteinase K from Beauveria brongniartii

Product number:

Purity: 95% (SDS-PAGE)

Units/mg protein: ≥30 U/mg (Enzymatic Activity Unit Definition: One unit will hydrolyze urea denatured hemoglobin to produce color equivalent to 1.0 micromole of tyrosine per minute at pH 7.5 at 37 ℃)

Storage and use:

Long-term storage temperature: -20℃, or not more than 4℃.

The enzyme powder can be transported at room temperature, for short periods.

Under proper storage conditions, the recommended retest period is three years.

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