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 37°C. RNase Activity: None detectable ribonuclease activity after 16 hrs incubation at 25°C.  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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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 37°C. RNase Activity: None detectable ribonuclease activity after 16 hrs incubation at 25°C.  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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Specific Activity: ≥ 2000 Kunitz units/mg Form: Lyophilized Powder Storage: 4°C DNase Ⅰ (RNase-free) is an endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products with 5´-phosphorylated and 3´-hydroxylated ends. DNase I acts on single- and double-stranded DNA, chromatin and RNA:DNA hybrids. Feature Recombinant enzyme Purified from non-animal host with a lower level of intrinsic RNases. Applications Degradation of DNA template in transcription reactions Removal of contaminating genomic DNA from RNA samples DNase I footprinting Nick Translation Quality Control The absence of ribonucleases is confirmed by appropriate quality test. Functionally tested for digestion of template DNA after in vitro transcription Source: A E. Coli strain that carries an MBP fusion clone of Bovine Pancreatic DNase I. Molecular Weight: 29 kDa monomer Definition of Activity Unit One unit of the enzyme completely degrades 1 μg of plasmid DNA in 10 min at 37°C. Enzyme activity is assayed in the following mixture: 40 mM Tris-HCl (pH 8.0), 10 mM MgSO4, 1 mM CaCl2, 1 μg of pUC19 DNA. Inhibition and Inactivation Inhibitors: metal chelators, transition metals (e.g., Zn) in millimolar concentrations, SDS (even at concentrations less than 0.1%), reducing agents (DTT and beta-mercaptoethanol), ionic strength above 50-100 mM. Inactivated by heating at 65°C for 10 min in the presence of EGTA or EDTA (use at least 1 mol of EGTA/EDTA per 1 mol of Mn2+/Mg2+). Note: DNase I is sensitive to physical denaturation. Mix gently by inverting the tube. Do not Vortex. Preparation InstructionsDNase I is soluble in 0.15 M NaCl at 5 mg/ml. Solutions of DNase I at 5 mg/ml in 0.15 M NaCl may lose 10% of its activity when stored for a week in aliquots at -20°C. The same solutions stored in aliquots at 2-8°C can lose 20% activity. Alternatively, solutions at a minimum concentration of 1 mg protein/ml, with 5 mM calcium chloride and stored at -20°C, may retain 90% activity for at least a year. Solutions containing 0.1 mg protein/ml are considerably less stable, and may require gelatin as stabilizer. For applications unaffected by glycerol, two other storage buffers are options, as these formulations do not freeze at -20°C. 20 mM sodium acetate (pH 6.5), containing 5 mM CaCl2 and 0.1 mM phenylmethylsulfonyl fluoride (PMSF), 50% (v/v) glycerol, with DNase I at 5 mg/ml. 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 10 mM MgCl2, 1 mM DTT, 50% (v/v) glycerol, with DNase I at 2 mg/ml.

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Specific Activity: ≥ 2000 Kunitz units/mg Form: Lyophilized Powder Storage: 4°C DNase Ⅰ (RNase-free) is an endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products with 5´-phosphorylated and 3´-hydroxylated ends. DNase I acts on single- and double-stranded DNA, chromatin and RNA:DNA hybrids. Feature Recombinant enzyme Purified from non-animal host with a lower level of intrinsic RNases. Applications Degradation of DNA template in transcription reactions Removal of contaminating genomic DNA from RNA samples DNase I footprinting Nick Translation Quality Control The absence of ribonucleases is confirmed by appropriate quality test. Functionally tested for digestion of template DNA after in vitro transcription Source: A E. Coli strain that carries an MBP fusion clone of Bovine Pancreatic DNase I. Molecular Weight: 29 kDa monomer Definition of Activity Unit One unit of the enzyme completely degrades 1 μg of plasmid DNA in 10 min at 37°C. Enzyme activity is assayed in the following mixture: 40 mM Tris-HCl (pH 8.0), 10 mM MgSO4, 1 mM CaCl2, 1 μg of pUC19 DNA. Inhibition and Inactivation Inhibitors: metal chelators, transition metals (e.g., Zn) in millimolar concentrations, SDS (even at concentrations less than 0.1%), reducing agents (DTT and beta-mercaptoethanol), ionic strength above 50-100 mM. Inactivated by heating at 65°C for 10 min in the presence of EGTA or EDTA (use at least 1 mol of EGTA/EDTA per 1 mol of Mn2+/Mg2+). Note: DNase I is sensitive to physical denaturation. Mix gently by inverting the tube. Do not Vortex. Preparation InstructionsDNase I is soluble in 0.15 M NaCl at 5 mg/ml. Solutions of DNase I at 5 mg/ml in 0.15 M NaCl may lose 10% of its activity when stored for a week in aliquots at -20°C. The same solutions stored in aliquots at 2-8°C can lose 20% activity. Alternatively, solutions at a minimum concentration of 1 mg protein/ml, with 5 mM calcium chloride and stored at -20°C, may retain 90% activity for at least a year. Solutions containing 0.1 mg protein/ml are considerably less stable, and may require gelatin as stabilizer. For applications unaffected by glycerol, two other storage buffers are options, as these formulations do not freeze at -20°C. 20 mM sodium acetate (pH 6.5), containing 5 mM CaCl2 and 0.1 mM phenylmethylsulfonyl fluoride (PMSF), 50% (v/v) glycerol, with DNase I at 5 mg/ml. 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 10 mM MgCl2, 1 mM DTT, 50% (v/v) glycerol, with DNase I at 2 mg/ml.

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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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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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