TGS1 Protein, Human (His-SUMO)

TGS1 protein plays a pivotal role in cellular processes by catalyzing the sequential methylation steps involved in the conversion of the 7-monomethylguanosine (m(7)G) caps of small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. This enzyme exhibits specificity for guanine, with N7 methylation preceding N2 methylation in the modification process. The hypermethylation of the m7G cap of U snRNAs results in their localization to nuclear foci, co-localization with coilin, and the formation of canonical Cajal bodies (CBs). Beyond its involvement in RNA modification, TGS1 also contributes to transcriptional regulation, underscoring its significance in cellular function. TGS1 Protein, Human (His-SUMO) is the recombinant human-derived TGS1 protein, expressed by E. coli , with N-His, N-SUMO labeled tag. The total length of TGS1 Protein, Human (His-SUMO) is 141 a.a., with molecular weight of ~31.6 kDa.

TGS1 protein plays a pivotal role in cellular processes by catalyzing the sequential methylation steps involved in the conversion of the 7-monomethylguanosine (m(7)G) caps of small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. This enzyme exhibits specificity for guanine, with N7 methylation preceding N2 methylation in the modification process. The hypermethylation of the m7G cap of U snRNAs results in their localization to nuclear foci, co-localization with coilin, and the formation of canonical Cajal bodies (CBs). Beyond its involvement in RNA modification, TGS1 also contributes to transcriptional regulation, underscoring its significance in cellular function.

Human

E. coli

N-His;N-SUMO

Q96RS0 (713M-853T)

96764  [NCBI]

MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWGGPDYATAETFDIRTMMSPDGFEIFRLSKKITNNIVYFLPRNADIDQVASLAGPGGQVEIEQNFLNNKLKTITAYFGDLIRRPASET

Approximately 31.6 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.