ASF/SF2 (alternative splicing factor/splicing factor 2)/splicing factor, arginine/serine-rich 1 (SFRS1) is a sequence specific (5'-splice cleavage) splicing factor involved in pre-mRNA splicing/alternative splicing. ASF/SF2 also mediates mRNA nuclear export and translation processes. ASF/SF2 supports genomic stability by impeding formation of mutagenic DNA:RNA hybrid R loop structures between the transcript and the template DNA. ASF/SF2 is involved in the replicaton of HIV-1.
Storage: -20C
Application: Anti-SFRS1 (AB1) polyclonal antibody is used to tag ASF/SF2 (alternative splicing factor/splicing factor 2)/ splicing factor, arginine/serine-rich 1 for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of ASF/SF2 in pre-mRNA splicing, mRNA export and translation and genome stabilization.
Biochem Physiol Actions: SFRS1 is a member of the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. The protein binds to pre-mRNA transcripts and components of the spliceosome, and can either activate or repress splicing depending on the location of the pre-mRNA binding site. The protein's ability to activate splicing is regulated by phosphorylation and interactions with other splicing factor associated proteins. Multiple transcript variants encoding different isoforms have been found for this gene.Alternative mRNA splicing plays an important role in development and differentiation; many transcripts are spliced differently in distinct cell types and tissues. Both constitutive and alternative splicing occurs on spliceosomes, which are complex particles composed of small nuclear ribonucleoproteins (snRNPs) and non-snRNP proteins. The SR family of non-snRNP splicing factors is characterized by the presence of an RNA recognition motif and a serine- and arginine-rich (SR) domain. SR proteins are required at early stages of spliceosome assembly, have distinct but overlapping specificities for different pre-mRNAs, and can alter splice site choice, suggesting that they may be involved in the regulation of alternative splicing in vivo. Two of the SR proteins, ASF/SF2 (SFRS1) and SC35 (SFRS2; MIM 600813), have been extensively characterized.Alternative mRNA splicing plays an important role in development and differentiation; many transcripts are spliced differently in distinct cell types and tissues. Both constitutive and alternative splicing occurs on spliceosomes, which are complex particles composed of small nuclear ribonucleoproteins (snRNPs) and non-snRNP proteins. The SR family of non-snRNP splicing factors is characterized by the presence of an RNA recognition motif and a serine- and arginine-rich (SR) domain. SR proteins are required at early stages of spliceosome assembly, have distinct but overlapping specificities for different pre-mRNAs, and can alter splice site choice, suggesting that they may be involved in the regulation of alternative splicing in vivo. Two of the SR proteins, ASF/SF2 (SFRS1) and SC35 (SFRS2; MIM 600813), have been extensively characterized (Bermingham et al., 1995).[supplied by OMIM].