Recombinant 2019-nCoV Guanine-N7_meth Protein (His Tag) | 763-PKSR030473

(No reviews yet) Write a Review
€278.00 - €569.00
Frequently bought together:


Recombinant 2019-nCoV Guanine-N7_meth Protein (His Tag) | PKSR030473 | Elabscience.

Synonym: SARS-CoV 2 nsp14; SARS-CoV 2 ExoN; Guanine-N7 methyltransferase

Activity: N/A

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.

Sequence: Ala1-Gln527

Fusion tag: N-6His

Accession: YP_009725309.1

Species: SARS-CoV-2

Expressed Host: E.coli

Shipping Conditions: 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.

Mol Mass: 62.9 kDa

AP Mol Mass: 60 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.

View AllClose