Cusao Proteinase k

Proteinase K, recombinant

Proteinase Okay – certainly one of many often used enzymes in molecular biology.

Wonderful totally different for protein digestion in varied options.

  • BLIRT – expert in Proteinase Okay manufacturing for over 15 years.
  • Licensed manufacturing course of ISO 13485 ensuing inside the best high-quality product with a extraordinarily low batch-to-batch variability.
  • Giant components, the possibility of white labeling, and portioning service – liquid kind inside the quantity on the client’s request (as quite a bit as lots of million samples month-to-month).

Thermo Scientific Proteinase Okay is a broad-range endolytic protease extensively used for digestion of proteins in nucleic acid preparations. It degrades proteins even contained in 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 Major Digestion of Protein in Pure Samples

  • Energetic over a pH vary 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 Straightforward to Use

  • Energetic over pH vary 4.3–12.Zero in 0.5% SDS or 1% Triton X-100
  • Retains >80% practice at temperatures as quite a bit as 60°C
  • No resuspension or thawing before use
  • Cat.# MC5005, MC5008 equipped at a highlight of 20mg/ml
Proteinase K, recombinant
Proteinase Ok, recombinant



Highlights



• Prepared-to-use reply
• Energetic in a variety of response circumstances

Options

• 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

Keep in mind



• The really useful working focus of Proteinase Okay is 0.05 to 1 mg/mL. The practice of the enzyme is stimulated by 0.2 to 1% SDS or by 1 to Four M urea
• Ca2+ protects Proteinase Okay within the course of autolysis, will improve the thermal stability, and has a regulatory perform for the substrate binding web site of Proteinase Okay
• Secure over an enormous pH vary: 4.Zero to 12.5, optimum pH 7.5 to eight.0
• Optimum practice 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 particular practice.

Recombinant Proteinase Okay enzyme is expressed in Pichia pastoris, and undergoes in depth purification to yield the right high-quality product.

Proteinase Okay Molecular Biology Grade (PCR Grade) is energetic beneath a variety of 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 via nucleic acid preparations with out compromising the integrity of remoted DNA or RNA.

Selections

  • Recombinant broad-spectrum non-specific protease derived from Tritirachium album and over-expressed in Pichia pastoris.
  • Excessive practice and distinctive purity.
  • Energetic at excessive temperatures (as quite a bit as 56 °C) and denaturing circumstances (e.g. contained in the presence of urea and/or SDS), which makes it highest for digesting proteins in quite a lot of options.
  • Secure over an enormous pH vary: 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.

Options:

  • Extraction of DNA and RNA from fully fully totally different beginning supplies.
  • Purification of goal provides from contaminating proteins.
  • Elimination of DNases and RNases all via nucleic acids isolation.

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Description: (FR)

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