Proteinase K, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity. It cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples. It has been purified to remove RNase and DNase activities. The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications including preparation of chromosomal DNA for pulsed-field gel electrophoresis, protein fingerprinting and removal of nucleases from preparations of DNA and RNA. A typical working concentration for Proteinase K is 50–100μg/ml.
Formulation: Proteinase K (PK) Solution is supplied at a concentration of 20mg/ml in 10mM Tris-HCl (pH 7.5), 1mM calcium chloride and 50% glycerol.
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＜プロメガクラブ対象製品※MC5005のみ＞
Proteinase Kは真菌類(Tritirachium album Limber)由来のセリンプロテアーゼで、広い切断活性を示します。脂肪族および芳香族アミノ酸のカルボキシル末端側のペプチド結合を切断し、生物学サンプルに含まれるタンパク質加水分解に汎用されます（1）。本酵素は精製されており、RNaseおよびDNase活性が除去されています。尿素およびSDS中での安定性や未変性タンパク質を分解する特性から、パルスフィールドゲル電気泳動に用いる染色体DNAの調製（2）、タンパク質フィンガープリンティング（3,4）、DNA（5）やＲＮＡ（6,7）の調製におけるヌクレアーゼの除去など様々なアプリケーションで有用です。標準的な使用濃度は50–100μg/mlです。
組成: Proteinase K(PK)Solutionの濃度は20mg/ml（in 10mM Tris-HCl(pH7.5),1mM calcium chloride and 50%glycerol）
- 安定性: 0.5%SDSまたは1%Triton®X-100、およびpH 4.3-12.0で活性を有し、最大60℃まで80%以上の活性を保持
- 使いやすい: 室温で安定な溶液タイプなので、再懸濁や使用前の融解が不要
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