TGS1 Protein, Human (His-SUMO)

TGS1 protein catalyzes the conversion of the 7-monomethylguanosine (m(7)G) cap of small nuclear RNA (snRNA) and small nucleolar RNA (snoRNA) into 2, 2,7-trimethylguanosine (m( 2,2,7)G) Cap structure. The enzyme shows specificity for guanine, with N7 methylation occurring before N2 methylation during the modification process. 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, or trimethylguanosine synthase 1, is a key enzyme that catalyzes two consecutive methylation steps essential for the conversion of 7-monomethylguanosine (m7G) caps present on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) to a 2,2,7-trimethylguanosine (m2,2,7G) cap structure. This process involves specific methylation of guanine at the N7 position followed by N2 methylation. The hypermethylation of the m7G cap on U snRNAs leads to their concentration in nuclear foci, colocalization with coilin, and the formation of canonical Cajal bodies (CBs). TGS1's involvement in these processes suggests its role in the regulation of transcription and the dynamic organization of nuclear structures. It has to highlight TGS1's specificity for guanine and its critical function in shaping the cap structure of RNA molecules, influencing cellular processes associated with RNA modification and localization.

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.