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Proteinase K Solution, 20mg/ml (10 ml)

    Description

    Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. The Proteinase K is classified as a serine protease. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.

    • Specific Activity: 40 U/mg protein
    • Molecular Weight: 28.9 kDa monomer
    • Source: Pichia pastoris cells with a cloned gene encoding Tritirachium album endolytic protease (Proteinase K).

    Applications

    • Isolation of genomic DNA from cultured cells and tissues
    • Removal of DNases and RNases when isolating DNA and RNA from tissues or cell lines 
    • Determination of enzyme localization
    • Improving cloning efficiency of PCR products 

    Quality Control

    • DNase Activity: None detectable enzyme activity with λ DNA after 6 hrs incubation at 37ºC.
    • RNase Activity: None detectable ribonuclease activity after 16 hrs incubation at 25ºC. 

    Dilution Buffer

    50 mM Tris-HCl (pH 7.5), containing 5 mM calcium chloride and 50% (v/v) glycerol. 

    Definition of Activity Unit

    One unit of the enzyme liberates Folin-positive amino acids and peptides corresponding to 1 µmol tyrosine in 1 min at 37°C using denatured hemoglobin as substrate.
    Enzyme activity is assayed in the following mixture: 0.08 M potassium phosphate (pH 7.5), 5 M urea, 4 mM NaCl, 3 mM CaCl2 and 16.7 mg/ml hemoglobin.

    Storage

    For long time storage, store the Proteinase K powder at 4ºC and solution at -20°C

    Inhibition and Inactivation

    • Inhibitors: Proteinase K is not inactivated by metal chelators, by thiol-reactive reagents or by specific trypsin and chymotrypsin inhibitors. Phenylmethylsulfonyl fluoride and diisopropyl phosphorofluoridate completely inhibit the enzyme.
    • Inactivated by heating at 95°C for 10 minutes. 

    Other Note:

    • Optimum activity at 50-55°C. 
    • Rapid denaturation of enzyme occurs at temperatures above 65°C. 
    • The recommended working concentration for Proteinase K is 0.05-1 mg/ml. The activity of the enzyme is stimulated by 0.2-1% SDS or by 1-4 M urea.
    • Ca2+ protects Proteinase K against autolysis, increases the thermal stability and has a regulatory function for the substrate binding site of Proteinase K.
    • Stable over a wide pH range: 4.0-12.5, optimum pH 7.5-8.0.
    Product form

    SKU: PK02-10ML

    Proteinase K Solution, 20mg/ml (10 ml)

      Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino... Read more

      $179.00

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          Description

          Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. The Proteinase K is classified as a serine protease. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.

          • Specific Activity: 40 U/mg protein
          • Molecular Weight: 28.9 kDa monomer
          • Source: Pichia pastoris cells with a cloned gene encoding Tritirachium album endolytic protease (Proteinase K).

          Applications

          • Isolation of genomic DNA from cultured cells and tissues
          • Removal of DNases and RNases when isolating DNA and RNA from tissues or cell lines 
          • Determination of enzyme localization
          • Improving cloning efficiency of PCR products 

          Quality Control

          • DNase Activity: None detectable enzyme activity with λ DNA after 6 hrs incubation at 37ºC.
          • RNase Activity: None detectable ribonuclease activity after 16 hrs incubation at 25ºC. 

          Dilution Buffer

          50 mM Tris-HCl (pH 7.5), containing 5 mM calcium chloride and 50% (v/v) glycerol. 

          Definition of Activity Unit

          One unit of the enzyme liberates Folin-positive amino acids and peptides corresponding to 1 µmol tyrosine in 1 min at 37°C using denatured hemoglobin as substrate.
          Enzyme activity is assayed in the following mixture: 0.08 M potassium phosphate (pH 7.5), 5 M urea, 4 mM NaCl, 3 mM CaCl2 and 16.7 mg/ml hemoglobin.

          Storage

          For long time storage, store the Proteinase K powder at 4ºC and solution at -20°C

          Inhibition and Inactivation

          • Inhibitors: Proteinase K is not inactivated by metal chelators, by thiol-reactive reagents or by specific trypsin and chymotrypsin inhibitors. Phenylmethylsulfonyl fluoride and diisopropyl phosphorofluoridate completely inhibit the enzyme.
          • Inactivated by heating at 95°C for 10 minutes. 

          Other Note:

          • Optimum activity at 50-55°C. 
          • Rapid denaturation of enzyme occurs at temperatures above 65°C. 
          • The recommended working concentration for Proteinase K is 0.05-1 mg/ml. The activity of the enzyme is stimulated by 0.2-1% SDS or by 1-4 M urea.
          • Ca2+ protects Proteinase K against autolysis, increases the thermal stability and has a regulatory function for the substrate binding site of Proteinase K.
          • Stable over a wide pH range: 4.0-12.5, optimum pH 7.5-8.0.

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