FUSIP1 Polyclonal Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND

Application
| WB, IHC-P, IHC-F, IF, ICC, E |
|---|---|
| Primary Accession | O75494 |
| Reactivity | Rat, Pig, Dog, Bovine |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 31 KDa |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human FUSIP1 |
| Epitope Specificity | 151-250/262 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SUBCELLULAR LOCATION | Nucleus speckle. Cytoplasm. |
| SIMILARITY | Belongs to the splicing factor SR family. Contains 1 RRM (RNA recognition motif) domain. |
| SUBUNIT | The phosphorylated but not the dephosphorylated form interacts with TRA2B/SFRS10. The dephosphorylated form interacts with SNRNP70. Isoform 1 and isoform 3 interact with FUS C-terminus. |
| Post-translational modifications | Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. Isoform 3 is phosphorylated on Ser-168. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | FUSIP1 is a member of the Serine/Arginine (SR) family of splicing factors. Members of the SR family all contain one or more RNA recognition motifs (RRM) and an SR-rich domain. SR factors are not only essential for constitutive splicing but also regulate splicing in a concentration-dependent manner by influencing the selection of alternative splice sites. Expressed in a variety of tissues with low expression in kidney, liver and heart, FUSIP1 localizes to the cytoplasm and nuclear speckles. In its dephosphorylated form (occurring during M phase of the cell cycle), FUSIP1 functions as a potent general repressor of pre-mRNA splicing and can interact with U1 SnRNP 70. In its phosphorylated form, FUSIP1 interacts with Tra-2∫ and, together, they may cooperate in the regulation of splicing. Four isoforms exist for FUSIP1. In neurons, FUSIP1 isoforms may act to either positively or negatively regulate alternative splicing. |
| Gene ID | 10772 |
|---|---|
| Other Names | Serine/arginine-rich splicing factor 10, 40 kDa SR-repressor protein, SRrp40, FUS-interacting serine-arginine-rich protein 1, Splicing factor SRp38, Splicing factor, arginine/serine-rich 13A, TLS-associated protein with Ser-Arg repeats, TASR, TLS-associated protein with SR repeats, TLS-associated serine-arginine protein, TLS-associated SR protein, SRSF10, FUSIP1, FUSIP2, SFRS13A, TASR |
| Target/Specificity | Widely expressed. |
| Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,ICC=1:100-500,IF=1:100-500,ELISA=1:5000-10000 |
| Storage | Store at -20 ℃ for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 ℃. |
| Name | SRSF10 |
|---|---|
| Synonyms | FUSIP1, FUSIP2, SFRS13A, TASR |
| Function | Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing (PubMed:11684676, PubMed:12419250, PubMed:14765198). Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70 (PubMed:14765198). Required for splicing repression in M-phase cells and after heat shock (PubMed:14765198). Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing (PubMed:26876937). Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator (PubMed:12419250). |
| Cellular Location | Nucleus speckle. Cytoplasm |
| Tissue Location | Widely expressed. |

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