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Potvrzuji
  1. Úvodní strana
  2. Reagencie
  3. Life Technologies / Fermentas
  4. PCR, qPCR, RT-PCR & dNTPs
  5. Preparation of template for PCR and RT-PCR
  6. Proteinase K (recombinant), PCR grade

Proteinase K (recombinant), PCR grade

Kód produktu: EO0491 Kód výrobce: EO0491 Kód dodavatele: {AF206C29-C900-444E-B574-B14445ED5531} Výrobce: Life Technologies Czech Republic s.r.o.
Proteinase K (recombinant), PCR grade
1 309,22 Kč
1 082,00 Kč bez DPH
do týdne
1 mL
Recombinant enzyme


Proteinase K (recombinant), PCR grade

Proteinase K is a broad-range endolytic protease widely used for digestion of proteins in nucleic acid preparations. It degrades proteins even in the presence of detergents.
Zobraz detailní popis

Detailní popis

Thermo Scientific 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 (see Reference 1). The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.

Highlights

  • Ready-to-use solution
  • Active in a wide range of reaction conditions

Applications

  • Isolation of genomic DNA from mouse tail
  • Isolation of genomic DNA from cultured cells
  • Removal of DNases and RNases when isolating DNA and RNA from tissues or cell lines (see References 2, 3)
  • Determination of enzyme localization (see​ Reference 4)
  • Improving cloning efficiency of PCR products (see​ Reference 5)

Note

  • The recommended working concentration of Proteinase K is 0.05 to 1 mg/mL. The activity of the enzyme is stimulated by 0.2 to 1% SDS or by 1 to 4 M urea (see​ Reference 3)
  • Ca2+ protects Proteinase K against autolysis, increases the thermal stability, and has a regulatory function for the substrate binding site of Proteinase K (see​ Reference 7)
  • Stable over a wide pH range: 4.0 to 12.5, optimum pH 7.5 to 8.0 (see​ Reference 8)
  • Optimum activity at 50 to55°C
  • Rapid denaturation of enzyme occurs at temperatures above 65°C
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.
Hazardous No
Inhibition
  • 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 (see Reference 1).
Molecular Weight 28.9 kDa monomer (see Reference 6)
Quality Control The absence of endo-, exodeoxyribonucleases, and ribonucleases confirmed by appropriate quality tests.
Source Pichia pastoris cells with a cloned gene encoding Tritirachium album endolytic protease (Proteinase K).
Storage Buffer The enzyme is supplied in: 10 mM Tris-HCl (pH 7.5), containing calcium acetate and 50% (v/v) glycerol.
Storage Condition -20 C

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