Recombinant Human SF2 protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, GSA, EMSA.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application GSA | Reactivity Reacts | Dilution info - | Notes - |
Application EMSA | Reactivity Reacts | Dilution info - | Notes - |
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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. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
ASF, SF2, SF2P33, SFRS1, OK/SW-cl.3, SRSF1, Serine/arginine-rich splicing factor 1, Alternative-splicing factor 1, ASF-1
Recombinant Human SF2 protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, GSA, EMSA.
pH: 7.9
Constituents: 20% Glycerol (glycerin, glycerine), 0.55% Ammonium sulphate, 0.476% HEPES, 0.0077% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00584% EDTA
purified by affinity column
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. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
Belongs to the splicing factor SR family.
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.
1 unit equals 1 nanogram of purified protein.
SF2 also known as Splicing Factor 2 or Alternative Splicing Factor 1 (ASF1) is a prototypical member of the SR protein family involved in mRNA splicing. It is approximately 33 kDa in mass. SF2 is expressed ubiquitously in the nucleus of eukaryotic cells where it plays a central role in the regulation of constitutive and alternative splicing processes.
SF2 acts as an important regulator of gene expression by facilitating the splicing of pre-mRNA participating in spliceosome assembly. It interacts with other splicing factors and RNA to form spliceosomal complexes essential for splicing fidelity and efficiency. The precise modulation of splicing by SF2 allows for the generation of diverse protein isoforms from a single gene contributing to protein diversity within the cell.
SF2 integrates into the RNA splicing pathway and is critical for splice site selection. It interacts with proteins such as U1 snRNP and U2AF65 influencing their binding to pre-mRNA. SF2 also plays roles in other key pathways like mRNA transport and translation thereby linking the splicing machinery with nuclear export and protein synthesis processes.
Abnormalities in SF2 levels or functions have been linked to various cancers and spinal muscular atrophy (SMA). Cancer cells often show altered SF2 expression leading to splicing anomalies that promote tumorigenesis. Additionally SF2's interaction with proteins like hnRNP A1 influences disease mechanisms as splicing factor dysregulation can disrupt normal cellular processes and facilitate the progression of disorders such as SMA.
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