SARS-CoV-2 NSP12 Recombinant Protein
- SKU:
- RPES7053
- Product Type:
- Recombinant Protein
- Species:
- Virus
Description
| Product Name: | SARS-CoV-2 NSP12 Recombinant Protein |
| Product Code: | RPES7053 |
| Size: | 50µg |
| Species: | SARS-CoV-2 |
| Expression Host: | E.coli |
| Synonyms: | SARS-CoV 2 nsp12,RNA-directed RNA polymerase,RdRp |
| Mol Mass: | 64kDa |
| AP Mol Mass: | 60 kDa |
| Tag: | N-Gst |
| Purity: | > 90 % as determined by reducing SDS-PAGE. |
| Endotoxin Level: | Please contact us for more information. |
| Bio Activity: | Testing in progress |
| Sequence: | Asp4891-Val5212 |
| Accession: | QHD43415.1 |
| Storage: | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
| Shipping: | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation: | Supplied as solution form in PBS, pH7.5 or lyophilized from PBS, pH7.5 Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution: | Please refer to the printed manual for detailed information. |
| Background: | The RdRp of SARS-CoV-2 is composed of a catalytic subunit known as nsp12 as well as two accessory subunits, nsp8 and nsp7. The structure of this RdRp has recently been reported; it is highly similar to the RdRp of SARS-CoV, a zoonotic coronavirus that spread into the human population in 2002. The nsp12 subunit contains an N-terminal nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain, an interface domain and a C-terminal RdRp domain. The RdRp domain resembles a right hand, comprising the fingers, palm and thumb subdomains that are found in all single-subunit polymerases. Subunits nsp7 and nsp8 bind to the thumb, and an additional copy of nsp8 binds to the fingers domain. Structural information is also available for nsp8–nsp7 complexes. |
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