2019-nCoV NSP14 Methyltransferase, Active

Recombinant SARS-CoV-2 (COVID-19) NSP14 Methyltransferase (5925-6452) was expressed in E. coli using a C-terminal His-tag. The Purity of the 2019-nCoV NSP14 was determined to be approx. 80% by densitometry, and molecular weight calculated to be approx. 60 kDa. The NSP14 assay was performed inhouse using the methyltransferase-Glo TM methyltransferase assay kit.

A bifunctional non-structural protein 14 (NSP14) coded by coronaviruses is crucial for the replication and transcription of viral particles.

Coronaviruses codes for a bifunctional non-structural protein 14 (NSP14) that is important for viral replication and transcription.

NSP14 contains an N-terminal exo-ribonuclease (ExoN) domain for proof reading during viral replication and a C-terminal N-7 methyltransferase (N7-MTase) domain for mRNA capping. NSP14 associates with several viral proteins.1

It can bind to NSP10 and the resulting complex exhibits enhanced ExoN activity in vitro.2 It can also bind to the polymerase complex (NSP12/NSP8/NSP7) forming a complex that retains all associated enzymatic activities.3

Product specification

Sample activity

Sample Activity Plot.

Sample Activity Plot. Image Credit: SignalChem Biotech

For specific information on a given lot, users can see the related technical datasheet.

Purity

Sample Purity Data.

Sample Purity Data. Image Credit: SignalChem Biotech

For specific information on a given lot, see the related technical datasheet.

Assay data

Storage, stability, and shipping

The product should be stored at −70 °C. For optimal storage, the targets can be aliquoted into smaller amounts following centrifugation and can be stored at the proposed temperature. For optimal performance, multiple freeze/thaw cycles and repeated handling and should be avoided.

Molecular weight

60 kDa

References

  1. Ma, Y. et al: Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. PNAS, USA. (2015), 112(30):9436–9441.
  2. Bouvet, M. et al: RNA 3′-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc Natl Acad Sci USA. (2012), 109:9372–9377.
  3. Subissi, L. et al: One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc Natl Acad Sci USA. (2014), 111:E3900–E3909.