GH4500, GH4507, GH4502, Proteinase K (GMP Grade, Normal Liquid & For NGS)
Recombinant Proteinase K in PCR Grade is a universal tool for the preparation of nucleic acid templates. Proteinase K, originally isolated from the fungus Tritirachium album, is a recombinant enzyme expressed in Pichia pastoris. It is a highly active serine endopeptidase related to subtilisin that does not exhibit any pronounced cleavage specificity.
Therefore, recombinant, PCR grade proteinase K is a universal tool for template preparation. The amino acid sequence and molecular structure of the recombinant enzyme and the native protease are identical. However, the recombinant proteinase K production process guarantees an enzyme of extraordinary reliability and purity that meets all the requirements of diagnostic manufacturers.
Particular emphasis has been placed on the low DNA content of the enzyme preparation, which makes the recombinant, PCR-grade Proteinase K ideal for isolating PCR and RT-PCR templates.
- Maximize the yield of target nucleic acids.
- Proteinase K is rigorously tested for the absence of nucleases.
- Experience stability and security.
- The solution is very stable and can be stored at room temperature for at least 18 months. The handling of the solution is safe and flexible.
Recombinant, PCR grade proteinase K digests native proteins very efficiently. This enzyme can be used to rapidly inactivate endogenous RNases and DNases during nucleic acid isolation. Proteinase K is particularly suitable for the isolation of native RNA and DNA from tissues and cell lines.
The enzyme promotes cell lysis by activating a bacterial autolytic factor. Proteinase K is also used to:
- Analysis of membrane structures by modifying proteins and glycoproteins on the cell surface.
- Cell debris removal during colony survey preparation.
- Treatment of tissue sections to ensure efficient probe infiltration during in situ hybridization.