Anti-Unrip/STRAP Antibody Picoband®

Unrip is also known as STRAP (Serine-threonine kinase receptor-associated protein) . It is anenzyme that in humans is encoded by the STRAP gene. It is mapped to 12p12.3. UNRIP is integrated into a complex with UNR or with the SMN complex in vivo in a mutually exclusive manner. It is concluded that UNRIP is the first component of the uridine-rich snRNP assembly machinery that associates with the SMN complex in a compartment-specific way, and it may play a crucial role in the intracellular distribution of the SMN complex.

Serine-threonine kinase receptor-associated protein; MAP activator with WD repeats; UNR-interacting protein; WD-40 repeat protein PT-WD; STRAP; MAWD, UNRIP

The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. .

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.