Enzymes

Inorganic Pyrophosphatase (Yeast) is derived from a recombinant <i>E.Coli</i> strain carrying <i>Saccharomyces cerevisiae</i> ppa gene. The enzyme catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. P₂O₇^-4 + H₂O + PPase 2HPO₄^-2 Inorganic Pyrophosphatase (yeast) could hydrolyze the inorganic pyrophosphate generated by nucleic acid amplification, in vitro transcription and other reactions, removing the inhibition of the inorganic pyrophosphate generated on the reaction system. The removal of pyrophosphate can shift the reaction equilibrium to the end of product formation, which is beneficial to increase the yield of synthetic product. RNA and DNA synthesis are examples of reactions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase.

Inorganic Pyrophosphatase (Yeast) is derived from a recombinant <i>E.Coli</i> strain carrying <i>Saccharomyces cerevisiae</i> ppa gene. The enzyme catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. P₂O₇^-4 + H₂O + PPase 2HPO₄^-2 Inorganic Pyrophosphatase (yeast) could hydrolyze the inorganic pyrophosphate generated by nucleic acid amplification, in vitro transcription and other reactions, removing the inhibition of the inorganic pyrophosphate generated on the reaction system. The removal of pyrophosphate can shift the reaction equilibrium to the end of product formation, which is beneficial to increase the yield of synthetic product. RNA and DNA synthesis are examples of reactions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase.

Inorganic Pyrophosphatase (Yeast) is derived from a recombinant <i>E.Coli</i> strain carrying <i>Saccharomyces cerevisiae</i> ppa gene. The enzyme catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. P₂O₇^-4 + H₂O + PPase 2HPO₄^-2 Inorganic Pyrophosphatase (yeast) could hydrolyze the inorganic pyrophosphate generated by nucleic acid amplification, in vitro transcription and other reactions, removing the inhibition of the inorganic pyrophosphate generated on the reaction system. The removal of pyrophosphate can shift the reaction equilibrium to the end of product formation, which is beneficial to increase the yield of synthetic product. RNA and DNA synthesis are examples of reactions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase.

mRNA Cap 2'-O-methyltransferase was derived from a recombinant <i>E.coli</i> strain that carries the gene for the vaccinia mRNA Cap 2'-O-Methyltransferase. This enzyme adds a methyl group at the 2'-O position of the first nucleotide adjacent to the cap structure at the 5' end of the RNA. The enzyme utilizes S-adenosylmethionine (SAM) as a methyl donor to methylate capped RNA (cap-0) resulting in a cap-1 structure. The Cap 1 structure can increase the translation efficiency, improving the expression of mRNA in transfection and microinjection experiments. This enzyme specifically requires RNA with an m7GpppN cap as substrate. It cannot utilize RNA with pN, ppN, pppN or GpppN at the 5'end. Capped RNA may be prepared via in vitro transcription using cap analog or through enzymatic capping using the Vaccinia Capping Enzyme.

mRNA Cap 2'-O-methyltransferase was derived from a recombinant <i>E.coli</i> strain that carries the gene for the vaccinia mRNA Cap 2'-O-Methyltransferase. This enzyme adds a methyl group at the 2'-O position of the first nucleotide adjacent to the cap structure at the 5' end of the RNA. The enzyme utilizes S-adenosylmethionine (SAM) as a methyl donor to methylate capped RNA (cap-0) resulting in a cap-1 structure. The Cap 1 structure can increase the translation efficiency, improving the expression of mRNA in transfection and microinjection experiments. This enzyme specifically requires RNA with an m7GpppN cap as substrate. It cannot utilize RNA with pN, ppN, pppN or GpppN at the 5'end. Capped RNA may be prepared via in vitro transcription using cap analog or through enzymatic capping using the Vaccinia Capping Enzyme.

mRNA Cap 2'-O-methyltransferase was derived from a recombinant <i>E.coli</i> strain that carries the gene for the vaccinia mRNA Cap 2'-O-Methyltransferase. This enzyme adds a methyl group at the 2'-O position of the first nucleotide adjacent to the cap structure at the 5' end of the RNA. The enzyme utilizes S-adenosylmethionine (SAM) as a methyl donor to methylate capped RNA (cap-0) resulting in a cap-1 structure. The Cap 1 structure can increase the translation efficiency, improving the expression of mRNA in transfection and microinjection experiments. This enzyme specifically requires RNA with an m7GpppN cap as substrate. It cannot utilize RNA with pN, ppN, pppN or GpppN at the 5'end. Capped RNA may be prepared via in vitro transcription using cap analog or through enzymatic capping using the Vaccinia Capping Enzyme.

Poly(A) Polymerase is a polymerase expressed by recombinant <i>E.coli</i>. The enzyme does not depend on the template and can catalyze the sequential incorporation of ATP into the 3' end of RNA in the form of AMP, that is, adding a polyadenosine tail to the 3' end of RNA. Poly(A) structure can improve the stability of RNA and improve the translation efficiency of mRNA in eukaryotic cells. Poly(A) polymerase has high tailing efficiency and can add 20-200 A bases to the 3' end of RNA.

Poly(A) Polymerase is a polymerase expressed by recombinant <i>E.coli</i>. The enzyme does not depend on the template and can catalyze the sequential incorporation of ATP into the 3' end of RNA in the form of AMP, that is, adding a polyadenosine tail to the 3' end of RNA. Poly(A) structure can improve the stability of RNA and improve the translation efficiency of mRNA in eukaryotic cells. Poly(A) polymerase has high tailing efficiency and can add 20-200 A bases to the 3' end of RNA.

Poly(A) Polymerase is a polymerase expressed by recombinant <i>E.coli</i>. The enzyme does not depend on the template and can catalyze the sequential incorporation of ATP into the 3' end of RNA in the form of AMP, that is, adding a polyadenosine tail to the 3' end of RNA. Poly(A) structure can improve the stability of RNA and improve the translation efficiency of mRNA in eukaryotic cells. Poly(A) polymerase has high tailing efficiency and can add 20-200 A bases to the 3' end of RNA.