Thermo Scientific Proteinase Okay is a broad-range endolytic protease extensively used for digestion of proteins in nucleic acid preparations. It degrades proteins even all through the presence of detergents. Proteinase Okay cleaves peptide bonds on the carboxylic sides of aliphatic, fragrant, or hydrophobic amino acids. The Proteinase Okay is classed as a serine protease. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.

Proteinase Okay (Lyophilized)

For Main Digestion of Protein in Pure Samples

  • Energetic over a pH differ of 4.3–12.0, in 0.5% SDS or 1% Triton® X-100
  • Purified to take away RNase and DNase actions

Secure at Room Temperature and Simple to Use

  • Energetic over pH differ 4.3–12.Zero in 0.5% SDS or 1% Triton X-100
  • Retains >80% put collectively at temperatures as tons as 60°C
  • No resuspension or thawing ahead of use
  • Cat.# MC5005, MC5008 provided at a highlight of 20mg/ml

Proteinase Okay – one among many usually used enzymes in molecular biology.

Nice absolutely completely completely different for protein digestion in assorted selections.

  • BLIRT – educated in Proteinase Okay manufacturing for over 15 years.
  • Licensed manufacturing course of ISO 13485 ensuing all through the perfect prime quality product with a extraordinarily low batch-to-batch variability.
  • Monumental parts, the potential for white labeling, and portioning service – liquid selection all through the quantity on the buyer’s request (as tons as quite a few million samples month-to-month).

 

Recombinant Proteinase K

Recombinant Proteinase Ok


Highlights

• Prepared-to-use reply
• Energetic in numerous response circumstances

Capabilities

• Isolation of genomic DNA from mouse tail
• Isolation of genomic DNA from cultured cells
• Elimination of DNases and RNases when isolating DNA and RNA from tissues or cell traces
• Dedication of enzyme localization
• Enhancing cloning effectivity of PCR merchandise

Be mindful

• The really useful working focus of Proteinase Okay is 0.05 to 1 mg/mL. The put collectively of the enzyme is stimulated by 0.2 to 1% SDS or by 1 to Four M urea
• Ca2+ protects Proteinase Okay in path of autolysis, will enhance the thermal stability, and has a regulatory perform for the substrate binding internet web page of Proteinase Okay
• Secure over a big pH differ: 4.Zero to 12.5, optimum pH 7.5 to eight.0
• Optimum put collectively at 50 to55°C
• Speedy denaturation of enzyme happens at temperatures above 65°C.

 

Proteinase Okay Molecular Biology Grade from Parengyodontium album (Tritirachium album) is a subtilisin-related serine protease. It’s a broad-spectrum endopeptidase with a extraordinarily excessive express put collectively.

Recombinant Proteinase Okay enzyme is expressed in Pichia pastoris, and undergoes in depth purification to yield one of the best prime quality product.

Proteinase Okay Molecular Biology Grade (PCR Grade) is full of life beneath numerous response circumstances, together with elevated temperatures and the presence of SDS. In consequence, this enzyme is extensively utilizing for the digestion of proteins, together with DNases and RNases, all by way of nucleic acid preparations with out compromising the integrity of remoted DNA or RNA.

Decisions

  • Recombinant broad-spectrum non-specific protease derived from Tritirachium album and over-expressed in Pichia pastoris.
  • Excessive put collectively and distinctive purity.
  • Energetic at excessive temperatures (as tons as 56 °C) and denaturing circumstances (e.g. all through the presence of urea and/or SDS), which makes it biggest for digesting proteins in quite a few selections.
  • Secure over a big pH differ: 4.0–12.5 (optimum pH 7.5–8.0).
  • Decreased quantity of host DNA (≤ 10 pg/mg / MBG or ≤ 0.1 pg/mg NGS).
  • Accessible as powder, lyophilized “cake” or liquid.

Capabilities:

  • Extraction of DNA and RNA from completely absolutely absolutely completely completely different beginning presents.
  • Purification of goal provides from contaminating proteins.
  • Elimination of DNases and RNases all by way of nucleic acids isolation.

 

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