|Other Names||Serine/arginine-rich splicing factor 3, Pre-mRNA-splicing factor SRP20, Splicing factor, arginine/serine-rich 3, SRSF3, SFRS3, SRP20|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Splicing factor that specifically promotes exon- inclusion during alternative splicing (PubMed:26876937). Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). Also functions as export adapter involved in mRNA nuclear export such as of histone H2A (PubMed:11336712, PubMed:18364396). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity (PubMed:11336712, PubMed:18364396). RNA-binding is semi-sequence specific (PubMed:17036044).|
|Cellular Location||Nucleus. Nucleus speckle. Cytoplasm. Note=Recruited to nuclear speckles following interaction with YTHDC1.|
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Provided below are standard protocols that you may find useful for product applications.
SFRS3 is a member of theserine/arginine (SR)-rich family of pre-mRNA splicing factors,which constitute part of the spliceosome. Each of these factorscontains an RNA recognition motif (RRM) for binding RNA and an RSdomain for binding other proteins. The RS domain is rich in serineand arginine residues and facilitates interaction between differentSR splicing factors. In addition to being critical for mRNAsplicing, the SR proteins have also been shown to be involved inmRNA export from the nucleus and in translation. Two transcriptvariants, one protein-coding and the other non-coding, have beenfound for this gene.
Verma, D., et al. J. Virol. 84(22):11781-11789(2010)Anko, M.L., et al. Nat. Struct. Mol. Biol. 17(8):962-970(2010)Escudero-Paunetto, L., et al. Virology 401(2):155-164(2010)Manley, J.L., et al. Genes Dev. 24(11):1073-1074(2010)Fingert, J.H., et al. Mol. Vis. 16, 596-601 (2010) :
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