• Product name

  • Description

    Rabbit polyclonal to SF2
  • Host species

  • Tested applications

    Suitable for: WB, IHC-P, ICC/IFmore details
  • Species reactivity

    Reacts with: Mouse, Rat, Human
    Predicted to work with: Cow, Pig
  • Immunogen

    Fusion protein corresponding to Human SF2 aa 1-248. NP_008855.1


    Database link: Q07955

  • Positive control

    • WB: HeLa, MCF7 and DU 145 cell extracts. Mouse spleen and thymus extracts. IHC-P: Rat lung tissue. Mouse esophagus tissue. Human lung cancer tissue. ICC/IF: U-2 OS cells.


  • Form

  • Storage instructions

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
  • Storage buffer

    pH: 7.30
    Preservative: 0.02% Sodium azide
    Constituents: PBS, 50% Glycerol
  • Concentration information loading...
  • Purity

    Affinity purified
  • Clonality

  • Isotype

  • Research areas


Our Abpromise guarantee covers the use of ab238523 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/500 - 1/2000. Predicted molecular weight: 28 kDa.
IHC-P 1/50 - 1/200.
ICC/IF 1/50 - 1/200.


  • Function

    Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors.
  • Sequence similarities

    Belongs to the splicing factor SR family.
    Contains 2 RRM (RNA recognition motif) domains.
  • Domain

    The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling.
  • Post-translational

    Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed.
    Arg-97 is dimethylated, probably to asymmetric dimethylarginine.
  • Cellular localization

    Cytoplasm. Nucleus speckle. In nuclear speckles. Shuttles between the nucleus and the cytoplasm.
  • Information by UniProt
  • Database links

  • Alternative names

    • Alternative splicing factor 1 antibody
    • Alternative-splicing factor 1 antibody
    • arginine/serine-rich 1 antibody
    • ASF 1 antibody
    • ASF antibody
    • ASF-1 antibody
    • ASF1 antibody
    • FLJ53078 antibody
    • MGC5228 antibody
    • P33 subunit antibody
    • Pre mRNA splicing factor SF2 P33 subunit antibody
    • pre-mRNA-splicing factor SF2 antibody
    • Serine/arginine-rich splicing factor 1 antibody
    • SF2 antibody
    • SF2P33 antibody
    • SFRS1 antibody
    • Splicing factor 2 alternate splicing factor antibody
    • Splicing factor 2 antibody
    • Splicing factor antibody
    • Splicing factor arginine/serine rich 1 antibody
    • SR Splicing factor 1 antibody
    • SRp30a antibody
    • srsf1 antibody
    • SRSF1_HUMAN antibody
    see all


  • U-2 OS (Human bone osteosarcoma epithelial cell line) cells stained for SF2 using ab238523 (Top panel, red) at a 1/50 dilution in ICC/IF. Counterstained with DAPI (Bottom panel, merge).

  • Paraffin-embedded human lung cancer tissue stained for SF2 with ab238523 at a 1/200 dilution in immunohistochemical analysis.

  • Paraffin-embedded mouse esophagus tissue stained for SF2 with ab238523 at a 1/100 dilution in immunohistochemical analysis.

  • All lanes : Anti-SF2 antibody (ab238523) at 1/1000 dilution

    Lane 1 : HeLa (Human epithelial cell line from cervix adenocarcinoma) cell extract
    Lane 2 : MCF7 (Human breast adenocarcinoma cell line) cell extract
    Lane 3 : DU 145 (Human prostate carcinoma cell line) cell extract
    Lane 4 : Mouse thymus extract
    Lane 5 : Mouse spleen extract

    Lysates/proteins at 25 µg per lane.

    All lanes : HRP Goat Anti-Rabbit IgG (H+L) at 1/10000 dilution

    Predicted band size: 28 kDa

    Blocking buffer: 3% non-fat dry milk in TBST.

  • Paraffin-embedded rat lung tissue stained for SF2 with ab238523 at a 1/100 dilution in immunohistochemical analysis.


ab238523 has not yet been referenced specifically in any publications.

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