Western blot analysis of STRAP on different lysates with Mouse anti-STRAP antibody (HA601007) at 1/500 dilution.
Lane 1: 293T cell lysate
Lane 2: Jurkat cell lysate
Lane 3: A549 cell lysate
Lysates/proteins at 10 µg/Lane.
Predicted band size: 38 kDa
Observed band size: 38 kDa
Exposure time: 2 minutes;
10% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (HA601007) at 1/500 dilution was used in 5% NFDM/TBST at room temperature for 2 hours. Goat Anti-Mouse IgG - HRP Secondary Antibody (HA1006) at 1:100,000 dilution was used for 1 hour at room temperature.
MAP activator with WD repeats antibody;MAWD antibody;PTWD antibody;Serine-threonine kinase receptor-associated protein antibody;serine/threonine kinase receptor associated protein antibody;strap antibody;STRAP_HUMAN antibody;UNR-interacting protein antibody;UNRIP antibody;WD 40 repeat protein PT WD antibody;WD-40 repeat protein PT-WD antibody
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and 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 (Sm core). 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. 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.
Just like the interactions between antigens and antibodies, the higher the affinity between you and us the better.