Anti-m3G-cap, m7G-cap Antibody, clone H-20

Descrição detalhada : The nucleotide structure named the 2,2,7-trimethylguanosine(m3G)-containing cap structure of small nuclear ribonucleoprotein particles, or U snRNPs is an essential part of mRNA processing. Each snRNP particle consists of one (U1, U2 and U5) or two (U4/U6) snRNA molecules, a common set of eight core proteins (B, B9, D1, D2, D3, E, F and G, also denoted Sm proteins) that are bound to each of the 2,2,7- trimethylguanosine (m3G) cap-containing snRNAs U1, U2, U4 and U5, and several proteins associated specifically with the individual U snRNPs. Except for U6 snRNP, which does not leave the nucleus, the synthesis of these U snRNPs requires the bidirectional transport of the snRNA across the nuclear envelope. The snRNAs U1, U2, U4 and U5 are synthesized in the nucleus with a 7-monomethylguanosine (m7G) cap structure whereas the Sm proteins are stored in the cytoplasm and do not migrate into the nucleus in the absence of bound U snRNA. Instead, newly transcribed U snRNAs are transiently exported into the cytoplasm where the Sm proteins bind the snRNA’s Sm site, to form a ribonucleoprotein complex referred to as the Sm core. Stable association of all Sm proteins is essential for the hypermethylation of the m7G-cap to the m3G-cap structure. After this event and processing of the snRNAs, the mature snRNP particles are transported back to the nucleus in a receptor-and energy-dependent manner and the complete particle is formed. Monoclonal H-20 recognizes both m3G cap containing snRNPs as well as m7G capped structures and it should have a wide application, not only for studying the molecular biology and immunology of the U snRNPs from diverse organisms, but also for the characterization and isolation of m7G-capped transcripts.
Armazenamento : -20°C
Embalagem : 1X1EA