SF2 Recombinant Rabbit monoclonal Antibody IgG

SKU: BA112542-100µl

Fig1: Western blot analysis of SF2 on different lysates using anti-SF2 antibody at 1/500 dilution.

 Positive control:

 Lane 1: Mouse heart 

  Lane 2: Mouse liver

 Lane 3: K562


Fig2: ICC staining SF2 in A431 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Fig3: Immunohistochemical analysis of paraffin-embedded human lung cancer tissue using anti-SF2 antibody. Counter stained with hematoxylin.

Bon Opus Cat. #BA112542
  • Host Species; Species Reactivity

    Rabbit; Human, Mouse, Rat
  • Immunogen

    Recombinant protein
  • Application Summary

  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Serine/arginine-rich splicing factor 1, Alternative-splicing factor 1, Splicing factor, arginine/serine-rich 1, pre-mRNA-splicing factor SF2, P33 subunit
  • Background

    Pre-mRNA splicing enhancer elements are short RNA sequences capable of activating weak splice sites in nearby introns that are required for accurate splice site recognition and the control of alternative splicing. Splicing enhancer elements contain specific binding sites for serine/arginine (SR)-rich splicing factors, which include SC35, 9G8, SRp20, and SF2/ASF. The family of SR factors all contain one or more RNA recognition motifs (RRM) and an arginine/ serine (RS)-rich domain. They are not only essential for constitutive splicing but also regulate splicing in a concentration-dependent manner by influencing the selection of alternative splice sites. The majority of SR proteins, including SC35 and SRp40, are confined to the nucleus, while SF2/ASF, SRp20, and 9G8 are continuously shuttled between the nucleus and the cytoplasm and contribute to mRNA transport. The activity of SR proteins in regulated splicing is antagonized by members of the hnRNP A/B family of proteins, which induce drastic shifts in the selection of splicing sites.(ET7107-70)

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