Description
Recombinant 2019-nCoV Guanine-N7_meth Protein (His Tag) | PKSR030473 | Gentaur US, UK & Europe Disrtribition
Synonyms: SARS-CoV 2 nsp14; SARS-CoV 2 ExoN; Guanine-N7 methyltransferase
Active Protein: N/A
Activity: Recombinant 2019-nCoV Guanine-N7 methyltransferase is produced by our E.coli expression system and the target gene encoding Ala1-Gln527 is expressed with a 6His tag at the N-terminus.
Protein Construction: Recombinant 2019-nCoV Guanine-N7 methyltransferase is produced by our E.coli expression system and the target gene encoding Ala1-Gln527 is expressed with a 6His tag at the N-terminus.
Fusion Tag: N-6His
Species: SARS-CoV-2
Expressed Host: E.coli
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 85 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 62.9 kDa
Formulation: Supplied as a 0.2 μM filtered solution of PBS, 10% Glycerol, pH 7.4.
Reconstitution: Not Applicable
Background: The nonstructural protein (nsp) 14 of SARS-CoV 2 was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). Nsp14 of coronaviruses two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. It may be involved in the proof-reading ability during the viral RNA replication and transcription. GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by nsp14.positive-stranded RNA genome of the coronaviruses is translated from ORF1 to yield polyproteins that are proteolytically processed into intermediate and mature nonstructural proteins (nsps). SARS-CoV 2 polyproteins incorporate 16 protein domains (nsps). The putative non-structural protein 2 (nsp2) of SARS-CoV plays an important role in viral transcription and replication, and is an attractive target for anti-SARS drug development.
Research Area: N/A
