Methyltransferase displays a Cytoplasmic domain capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m7GTP or m7GDP. GMP, GpppG, and GpppA were poor substrates for the methyltransferase. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m7GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure. Cap analogs such as m7GTP, m7GDP, et2m7GMP, and m2et7GMP inhibit the methyltransferase reaction. RNA-directed RNA polymerase plays an essential role in the virus replication. Binds to the 3-end of the genomic RNA, probably to initiate replication. Source: Recombinant protein corresponding to aa60-240 from hepatitis E virus genotype 1 ORF1, fused to His-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~24.4kD Amino Acid Sequence: EVFWNHPIQRVIHNELELYCRARSGRCLEIGAHPRSINDNPNVVHRCFLRPAGRDVQRWYTAPTRGPAANCRRSALRGLPAADRTYCFDGFSGCNFPAETGIALYSLHDMSPSDVAEAMFRHGMTRLYAALHLPPEVLLPPGTYRTASYLLIHDGRRVVVTYEGDTSAGYNHDVSNLRSWI Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.
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