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Poly(A) Polymerase

  • Cat.No.ON-126
  • SourceRecombinant E.coli
  • Purity>95% by SDS-PAGE
  • Storage-20℃
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Product description: Poly(A) Polymerase uses ATP as a substrate for template-independent addition of adenosine monophosphate to the 3'-hydroxyl termini of RNA molecules.

Source: Recombinant E.coli

Concentration and Size: 5U/μL

Unit Definition: One unit is defined as the amount of enzyme required to catalyze the incorporation of 10 nmoles of dNTPs into acid insoluble material in 30 minutes at 75℃.

Storage Buffer: 50mM Tris-HCl (pH8.2), 0.1mM EDTA, 1mM DTT, 0.1%(v/v) Tween-20, 0.1%(v/v) NP-40, 50%(v/v) glycerol.

Companion Product: 10X pfu Reaction Buffer, ON-068, 200mM Tris-HCl(pH8.8 at 25℃),100mM KCl, 100mM (NH4)2SO4, 20mM MgSO4, 1%Triton X-100

Related Products:

High Yield T7 RNA Synthesis Kit, Cat#ON-040

pfu DNA polymerase, Cat#ON-051

Taq DNA polymerase, Cat#ON-007

Ribonuclease Inhibitor, Human Placenta, Cat#ON-039

10X poly(A) Polymerase Reaction Buffer, Cat#ON-127

Protocol: The standard reaction will produce ~150bp long poly(A)-tail on up to 10ug of capped or uncapped RNA from IVT reactions and co-transcriptional capping reactions need to be purified before adding to the poly(A)-tailing reaction.

1. Combine the following reagents:

10X poly(A) Polymerase Reaction Buffer2μL
Poly(A) polymerase1μL
(Optional) RNase inhibitor20units
Nuclease-free H2Oto 20μL

2. Incubate reaction at ?37°C for 60 minutes.

3. Stop reaction by adding EDTA to final concentration of >11mM.

* Before poly(A)-tail reaction, heat-denaturation of the RNA may improve the efficiency of adding poly(A)-tail.

Storage Conditions: -20℃

Quality Assurance: Free of endonuclease, exonuclease and RNase activities.

Physical Purity: >95% by SDS-PAGE.

1. Bernstein P and Ross J (1989) Poly(A), poly(A) binding protein and the regulation of mRNA stability. Trends Biochem Sci 14: 373–377.

2. Gallie DR (1991) The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev 5: 2108–2116.

3. Krug, M.S. and Berger, S.L. (1987) Methods Enzymol. 152, 262.

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