Overview

Description

  • Nature

    Recombinant
  • Source

    Baculovirus infected insect cells
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Sequence

      MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH HHHH
    • Molecular weight

      29 kDa
    • Amino acids

      1 to 248
    • Tags

      His tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab219488 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • Endotoxin level

    < 1.000 Eu/µg
  • Purity

    > 95 % SDS-PAGE.
    Purified by using conventional chromatography techniques.
  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    pH: 8
    Constituents: 0.32% Tris HCl, 0.02% DTT, 0.75% Potassium chloride, 40% Glycerol, 0.01% EDTA

General Info

  • Alternative names

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

    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

Images

  • 15% SDS-PAGE - Recombinant Human SF2 protein (His tag) (ab219488) at 3 μg.

References

This product has been referenced in:

See 1 Publication for this product

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