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Vaccinia virus capping enzyme
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Molecular Biological Enzymes
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Product Description
Capping enzyme is a recombinant protein derived from vaccinia virus expressed and purified by E. coli. It can specifically add 7-methylguanylic acid cap structure (cap 0) to the 5'end of RNA.
The terminal cap structure helps to stabilize, transport and translate eukaryotic mRNA.
The capping enzyme is composed of D1R and D12L double subunits and has three enzymatic activities (D1R methyl has RNA triphosphatase and guanylate transferase activity; D12L methyl has guanine methyltransferase activity). In vitro transcription, the capping process requires capping enzyme, GTP, and methyl donor (SAM).
Source: Recombinant Escherichia coli (vaccinia virus)
Specification: 10 U/ul;
Definition of activity unit: Under the condition of 37°C, the amount of enzyme used to chimeric 10 pmol of (a32) GTP to 80 nt transcription product in 1 hour is 1 U.
Storage temperature: -20℃
Enzyme storage buffer: 20mM Tris-HCl (PH8.0), 0.1mM EDTA, 100mM NaCl, 1mM DTT, 0.1%(v/v) Triton X-100, 50%(v/v) glycerol
Quality control test: no Endonuclease, Nickase, Exonuclease, Rnase contamination.
Purity: SDS-PAGE: ≥99%
Precautions:
1. The reaction system cannot contain EDTA;
2. If ribonuclease inhibitor is added for the stability of RNA, add 0.5ul ribonuclease inhibitor (40U/ul) according to the reaction system in the manual;
3. In PH7.0-8.0, SAM is unstable, SAM should be added last;
4. Before the reaction, the RNA should be heat-treated to ensure that the 5'end secondary structure of the transcription product is opened.
Operation Manual:
1. Add RNA to a 1.5ml centrifuge tube without nuclease polluting the water;
2. 65℃, 5 minutes;
3. Ice bath for 5 minutes;
4. Add the following solutions in order:
Capping enzyme is a recombinant protein derived from vaccinia virus expressed and purified by E. coli. It can specifically add 7-methylguanylic acid cap structure (cap 0) to the 5'end of RNA.
The terminal cap structure helps to stabilize, transport and translate eukaryotic mRNA.
The capping enzyme is composed of D1R and D12L double subunits and has three enzymatic activities (D1R methyl has RNA triphosphatase and guanylate transferase activity; D12L methyl has guanine methyltransferase activity). In vitro transcription, the capping process requires capping enzyme, GTP, and methyl donor (SAM).
Source: Recombinant Escherichia coli (vaccinia virus)
Specification: 10 U/ul;
Definition of activity unit: Under the condition of 37°C, the amount of enzyme used to chimeric 10 pmol of (a32) GTP to 80 nt transcription product in 1 hour is 1 U.
Storage temperature: -20℃
Enzyme storage buffer: 20mM Tris-HCl (PH8.0), 0.1mM EDTA, 100mM NaCl, 1mM DTT, 0.1%(v/v) Triton X-100, 50%(v/v) glycerol
Quality control test: no Endonuclease, Nickase, Exonuclease, Rnase contamination.
Purity: SDS-PAGE: ≥99%
Precautions:
1. The reaction system cannot contain EDTA;
2. If ribonuclease inhibitor is added for the stability of RNA, add 0.5ul ribonuclease inhibitor (40U/ul) according to the reaction system in the manual;
3. In PH7.0-8.0, SAM is unstable, SAM should be added last;
4. Before the reaction, the RNA should be heat-treated to ensure that the 5'end secondary structure of the transcription product is opened.
Operation Manual:
1. Add RNA to a 1.5ml centrifuge tube without nuclease polluting the water;
2. 65℃, 5 minutes;
3. Ice bath for 5 minutes;
4. Add the following solutions in order:
| Denatured RNA | 15ul |
| 10* capping solution | 2ul |
| GTP（10mM） | 1ul |
| SAM（2mM） | 1ul |
| Capping enzyme | 1ul |
| Total capacity | 20ul |
5. 37℃, 30 minutes;
6. The capping is completed.
6. The capping is completed.
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