BD Transduction Laboratories™ Purified Mouse Anti-SRPK2

Mammalian cell pre-mRNA splicing is mediated by the spliceosome, a multi-component complex that contains two types of splicing factors: small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP factors. Interactions between snRNPs and pre-mRNA ensures proper establishment of a catalytic core for the splicing reaction. However, these interactions are mediated by the non-snRNP factors. The superfamily of Arg/Ser-rich (RS) domain containing splicing factors are well known non-snRNPs. All of these proteins share a similar structure consisting of an N-terminal RNA recognition motif and a C-terminal RS domain. However, different SR factors have distinct specificities and their function is regulated by their level of expression and by reversible phosphorylation. Two families of kinases phosphorylate RS domain-containing proteins: SR protein-specific kinases (SRPK1 and 2) and Clk/Sty. SRPK1 is predominate in the pancreas, whereas SRPK2 is highly expressed in brain. SRPK2 contains an N-terminal proline-rich sequence that mediates its in vitro interaction with a WW domain containing protein. SRPKs affect splice-site selection and are thought to affect alternative splicing.

This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.