SRSF1 Antibody

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Product Specs

Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze / thaw cycles.
Lead Time
Typically, we can ship your order within 1-3 business days of receiving it. Delivery times may vary depending on the method of purchase and location. For specific delivery information, please contact your local distributor.
Synonyms
Alternative splicing factor 1 antibody; Alternative-splicing factor 1 antibody; arginine/serine-rich 1 antibody; ASF 1 antibody; ASF antibody; ASF-1 antibody; ASF1 antibody; FLJ53078 antibody; MGC5228 antibody; P33 subunit antibody; Pre mRNA splicing factor SF2 P33 subunit antibody; pre-mRNA-splicing factor SF2 antibody; Serine/arginine-rich splicing factor 1 antibody; SF2 antibody; SF2P33 antibody; SFRS1 antibody; Splicing factor 2 alternate splicing factor antibody; Splicing factor 2 antibody; Splicing factor antibody; Splicing factor arginine/serine rich 1 antibody; SR Splicing factor 1 antibody; SRp30a antibody; srsf1 antibody; SRSF1_HUMAN antibody
Target Names
Uniprot No.

Target Background

Function
SRSF1 plays a crucial role in preventing exon skipping, ensuring accurate splicing, and regulating alternative splicing. It interacts with other spliceosomal components through its RS domains, forming a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. SRSF1 can stimulate the binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. It binds to purine-rich RNA sequences, including the octamer, 5'-RGAAGAAC-3' (r=A or G), or the decamers, AGGACAGAGC/AGGACGAAGC. Notably, it exhibits preferential binding to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer form a potent splicing enhancer in vitro, known as the ASF/SF2 splicing enhancer (ASE), which specifically activates ASE-dependent splicing. Isoforms ASF-2 and ASF-3, on the other hand, function as splicing repressors. SRSF1 may also act as an export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
Gene References Into Functions
  1. SRSF1 promotes vascular smooth muscle cell (VSMC) proliferation and injury-induced neointima formation. It favors the induction of a truncated p53 isoform, Delta133p53, which has an equal proliferative effect and, in turn, transcriptionally activates Kruppel-like factor 5 (KLF5) via the Delta133p53-EGR1 complex. This results in accelerated cell-cycle progression and increased VSMC proliferation. PMID: 28799539
  2. Repeated RNA-sequestration of SRSF1 triggers the NXF1-dependent nuclear export of C9ORF72 transcripts retaining expanded hexanucleotide repeats. PMID: 28677678
  3. A -44 G to A "hot zone" putative functional noncoding variant of SRSF1 was found in an AML patient. This variant alters the binding activities of E2F6, ELF1, and ELK4. PMID: 29764005
  4. The ability of SRPK1 to mobilize SRSF1 from speckles to the nucleoplasm depends on active CLK1. This mobilization is facilitated by the formation of an SRPK1-CLK1 complex, which enhances the phosphorylation of several serine-proline dipeptides in SRSF1. PMID: 29335301
  5. Mir505-3p inhibits tumor proliferation driven by SRSF1 in two neural tumor cell lines, Neuro-2a (N2a) and U251, specifically in serum-reduced conditions. This suggests that SRSF1 expression is promoted by increasing serum concentrations. PMID: 29120871
  6. The tumor suppressor miR30c may be involved in prostate cancer tumorigenesis, potentially by targeting ASF/SF2. PMID: 28677791
  7. SF2/ASF likely has a protective role against JC virus reactivation in multiple sclerosis patients. PMID: 27812788
  8. Immune suppression of JC virus gene expression is mediated by SRSF1. PMID: 26951564
  9. ASF/SF2 is identified as a splicing regulator of cyclin T1, contributing to the control of subsequent transcription events. PMID: 28422315
  10. MALAT1 increases AKAP-9 expression by promoting SRPK1-catalyzed SRSF1 phosphorylation in CRC cells. This finding reveals a novel mechanism by which MALAT1 regulates AKAP-9 expression in CRC cells. PMID: 26887056
  11. High levels of SF2, as a novel oncoprotein in RCC, are significantly associated with poor survival in a large cohort of RCC specimens. This study provides a roadmap for the prediction and validation of the miR-766-3p/SF2 axis, offering a therapeutic avenue for further RCC progression. PMID: 28657135
  12. A joint atomistic molecular dynamics (MD) and experimental study of two RRM-containing proteins, Fox-1 and SRSF1, bound with their single-stranded target RNAs, was conducted. Simulations revealed specific participation of Arg142 at the protein-RNA interface of the SRFS1 complex, subsequently confirmed by NMR and ITC measurements. PMID: 27193998
  13. NMR spectroscopy with two separately expressed domains of SRSF1 demonstrated interactions between residues in the RNA-binding motif 2 and the N-terminal region of the RS domain (RS1). PMID: 27091468
  14. SRSF1 morphants exhibited reduced bone cartilage formation in the brain and a dramatic reduction in Nkx-2.5 expression in the heart. Additionally, a significant decrease in functional chordin RNA was observed in SRSF1 morphants, suggesting that chordin is a target of SRSF1. These findings indicate that SRSF1 is essential for pattern formation, including heart, cartilage, and germ layer development. PMID: 27396620
  15. The study strongly supports SRSF1 as a prognostic biomarker in SCLC and provides a rationale for personalized therapy in SCLC. PMID: 27093186
  16. NSrp70 acts as a new molecular counterpart for alternative splicing of target RNA, counteracting SRSF1 and SRSF2 splicing activity. PMID: 26797131
  17. A potential mechanism involving the essential splicing factor ASF/SF2 through which morphine regulates splicing specificity of the MOR encoding gene, OPRM1, was identified for the first time. PMID: 26553431
  18. Global splicing analysis using RNA-seq revealed that exons carrying the hnRNP H-binding GGGGG motif are more likely to be skipped compared to those carrying the SRSF1-binding GGAGG motif in both human and mouse brains. PMID: 26282582
  19. Experimental evidence indicates that splicing factor SRSF1, SRSF2, U2AF35, U2AF65, and KHSRP expression levels in gastrointestinal tract tumors (colon, gastric, and pancreatic) differ compared to healthy tissues and cell lines. PMID: 26406946
  20. These findings reveal a molecular interplay between cellular SRSF1 and viral T-antigen in controlling JC virus gene expression. PMID: 26596376
  21. Alternative splicing of SRSF1 itself is a significant regulatory event. PMID: 26273603
  22. SF2 contributes to elevated ERK activation levels in hepatocellular carcinoma cells by modulating key components downstream of growth factor receptors and upstream of ERK. PMID: 26018840
  23. MALAT1 may function as a promoter of gastric cancer cell proliferation, partly by regulating SF2/ASF. PMID: 24857172
  24. SRSF1 regulates CD3zeta expression in human T cells and may contribute to the T cell defect in systemic lupus erythematosus. PMID: 26134847
  25. Serine/arginine-rich splicing factor 1 (SRSF1) specifically interacts with RIG-I to facilitate RIG-I-mediated production of type-I IFN triggered by cytosolic DNA. PMID: 25658361
  26. Using RNA-sequencing and 3-D cell cultures that mimic breast cancer, SRSF1-regulated alternative splicing targets were identified, which are candidates for mediating SRSF1's oncogenic functions in mammary cells. PMID: 26431027
  27. The accumulated knowledge about SRSF1 provides critical insight into its integral role in maintaining cellular homeostasis and suggests new targets for anticancer therapy. PMID: 24807918
  28. Proline phosphorylation by CLK1/CDC-like kinase 1, but not by SRPK1/serine/arginine-rich splicing factor kinase 1, regulates the conformation and alternative splicing function of SFRS1 (serine/arginine-rich splicing factor 1). PMID: 25529026
  29. SRSF1 is a critical regulator that controls both RNA splicing and stability in the nucleus and functions in a Malat1-dependent manner. PMID: 24468535
  30. Upon T cell activation, SRSF1 becomes limiting, and its function in CD6 exon 5 splicing is counteracted by an increase in CD6 transcription, dependent on chromatin acetylation. PMID: 24890719
  31. Armadillo repeat protein ARVCF interacts with the splicing factors SRSF1 (SF2/ASF), the RNA helicase p68 (DDX5), and the heterogeneous nuclear ribonucleoprotein hnRNP H2. PMID: 24644279
  32. Within the broader context of cancer pathology, SRSF1 plays a central role not only in the tumor cells but also in the surrounding stroma. PMID: 23966470
  33. This study demonstrates a novel mechanism of regulation of the splicing factor SRSF1 in human T cells and a potential molecular mechanism that controls its expression in SLE. PMID: 24368769
  34. New splicing events regulated by the oncogenic splicing factor SRSF1 in lung cancer were identified using a novel analytical tool. PMID: 24371231
  35. Specific induction of AS2 due to alternative splicing is associated with epithelial ovarian cancer. PMID: 23748175
  36. Overexpression of SRSF1 and SRSF9 promotes beta-catenin accumulation by recruiting beta-catenin mRNA and enhancing its translation in an mTOR-dependent manner. PMID: 23592547
  37. The data establish a new view of SRSF1 protein regulation where SRPK1 and CLK1 partition activities based on Ser-Pro versus Arg-Ser placement rather than on N- and C-terminal preferences along the RS domain. PMID: 23707382
  38. ASF/SF2 binds to a purine-rich region distant from both the previously published initiation site of HDV mRNA transcription and the binding site of RNAP II, suggesting it is not involved in HDV replication. PMID: 23349975
  39. This study describes a new mechanism of posttranscriptional regulation of DIO1 and demonstrates deregulation of DIO1 expression in pituitary adenoma, possibly due to disturbed expression of SF2/ASF. PMID: 23462647
  40. High expression of ASF is associated with chronic myeloid leukemia. PMID: 23228155
  41. SF2/ASF regulates IL-2 production, and decreased SF2/ASF expression in systemic lupus erythematosus (SLE) T cells contributes to deficient IL-2 production. PMID: 23319613
  42. SRSF1 serves as an anti-apoptotic factor and potentially contributes to leukemogenesis in pediatric ALL patients by cooperating with PRMT1. PMID: 22839530
  43. Depletion of SRSF1 in human cells compromises the association of splicing factors to nuclear speckles and influences the levels and activity of other SR proteins. PMID: 22855529
  44. SRSF1 is a direct target of the transcription factor oncoprotein MYC. PMID: 22545246
  45. Overexpression of SRSF1 rescues apoptosis of MCF-7 cells induced by Pnn depletion. PMID: 22454513
  46. In three-dimensional (3D) culture, SRSF1-overexpressing MCF-10A cells formed larger acini than control cells, reflecting increased proliferation and delayed apoptosis during acinar morphogenesis. PMID: 22245967
  47. ASF/SF2 translocates to the cytosol and regulates the alternative splicing of endoglin during senescence of endothelial cells. PMID: 21668763
  48. A novel intronic splicing enhancer that regulates caspase 9 RNA splicing and specifically interacts with SRSF1 was identified. PMID: 21622622
  49. Negative regulation of the JC virus promoter by SF2/ASF may control reactivation of JCV replication in the brain. PMID: 21297941
  50. Phosphorylation of the RS domain in SRSF1 induces a key molecular switch from intra- to intermolecular interactions, suggesting a plausible mechanism for the documented requirement for the phosphorylation/dephosphorylation cycle during pre-mRNA splicing. PMID: 21536904

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Database Links

HGNC: 10780

OMIM: 600812

KEGG: hsa:6426

STRING: 9606.ENSP00000258962

UniGene: Hs.68714

Protein Families
Splicing factor SR family
Subcellular Location
Cytoplasm. Nucleus speckle.

Q&A

What is SRSF1 and why is it significant for molecular biology research?

SRSF1, previously known as SF2/ASF, is a multifunctional RNA-binding protein belonging to the serine/arginine-rich (SR) protein family. It plays critical roles in several aspects of RNA metabolism:

SRSF1 primarily functions as a pre-mRNA splicing regulator, influencing both constitutive and alternative splicing patterns. As a shuttling protein, it moves between the nucleus and cytoplasm, participating in mRNA export. In the cytoplasm, SRSF1 serves as a translational activator for specific mRNAs, directly impacting protein synthesis .

Recent research has revealed SRSF1's involvement in cell cycle regulation, particularly affecting spindle, kinetochore, and M-phase proteins essential for accurate chromosome segregation . Additionally, SRSF1 has emerged as a key factor in cancer biology, immune response modulation, and viral replication mechanisms .

The significance of SRSF1 extends to its tight regulation within cells. SRSF1 expression is subject to negative autoregulation through multiple layers of post-transcriptional and translational control, highlighting its critical role in cellular homeostasis . This complex regulatory network ensures that SRSF1 levels remain properly balanced, as both overexpression and depletion can significantly impact cellular function.

What types of SRSF1 antibodies are available for research applications?

Several types of SRSF1 antibodies are available, varying in their epitope recognition, host species, and validated applications:

  • Epitope-specific antibodies:

    • N-terminal targeted antibodies recognizing amino acids 6-33 or 11-38

    • C-terminal targeted antibodies recognizing amino acids 158-186

    • Phosphorylation-specific antibodies (e.g., detecting phosphorylated Ser1)

  • Based on host organism and clonality:

    • Rabbit polyclonal antibodies (most common, offering broad epitope recognition)

    • Mouse monoclonal antibodies (providing consistent lot-to-lot reproducibility)

  • Application-optimized antibodies:

    • Western blotting (WB) validated antibodies

    • Immunohistochemistry (IHC-P) optimized antibodies for paraffin-embedded sections

    • Immunofluorescence (IF) validated antibodies

    • Flow cytometry (FACS) compatible antibodies

    • Immunoprecipitation (IP) validated antibodies

When selecting an SRSF1 antibody, researchers should consider species reactivity requirements. Many antibodies show reactivity with human, mouse, and rat SRSF1, but cross-reactivity varies between products. Some antibodies demonstrate broader cross-reactivity with zebrafish, guinea pig, cow, and other species, making them suitable for comparative studies .

The immunization strategy and purification method also impact antibody performance. Some antibodies are generated using synthetic peptides corresponding to specific regions (e.g., AA 6-33 VIRGPAGNNDCRIYVGNLPPDIRTKDIE), while others may use recombinant protein. Purification methods range from immunogen affinity purification to ammonium sulfate precipitation followed by dialysis .

How do I choose the right SRSF1 antibody for my specific application?

Selecting the appropriate SRSF1 antibody requires careful consideration of several factors to ensure optimal results for your specific experimental needs:

  • Experimental technique compatibility:

    • For Western blotting: Most SRSF1 antibodies perform well, but verify validation data shows a clear band at approximately 28 kDa with minimal background

    • For IHC/IF: Select antibodies specifically validated for these applications as they require recognition of the native protein conformation

    • For flow cytometry: Choose antibodies validated for FACS that can detect SRSF1 after fixation and permeabilization

    • For IP experiments: Select antibodies that demonstrate high affinity and specificity in immunoprecipitation assays

  • Epitope accessibility considerations:

    • N-terminal antibodies (AA 6-33) may be preferred if the C-terminus might be involved in protein-protein interactions

    • C-terminal antibodies (AA 158-186) may be better if studying interactions that involve the N-terminus

    • Consider potential post-translational modifications that might mask specific epitopes

  • Species reactivity requirements:

    • Verify that the antibody has been validated in your experimental organism

    • For cross-species studies, select antibodies with confirmed reactivity across your species of interest

    • Note that epitope conservation can vary between species - for example, some N-terminal antibodies target sequences that are identical between human and mouse SRSF1

  • Clonality considerations:

    • Polyclonal antibodies offer the advantage of recognizing multiple epitopes, potentially providing stronger signals

    • Monoclonal antibodies provide greater specificity and lot-to-lot consistency for longitudinal studies

  • Validation evidence:

    • Review publications that have used the antibody in applications similar to yours

    • Check for validation data showing antibody specificity through knockdown/knockout controls

    • Assess cross-reactivity information with other SR proteins, particularly if studying cells with altered SRSF1 levels, as SRSF1 depletion can increase levels of other SR proteins like SRSF2 and SRSF3

When possible, validate antibody performance in your experimental system before proceeding with full-scale experiments. This might involve comparing multiple antibodies, using positive controls (cells known to express SRSF1) and negative controls (SRSF1-depleted samples) to ensure specific detection.

What are the most common applications for SRSF1 antibodies in RNA biology research?

SRSF1 antibodies serve as essential tools in various aspects of RNA biology research, enabling investigations into splicing regulation, RNA-protein interactions, and translational control:

  • Protein expression and localization analysis:

    • Western blotting to quantify SRSF1 protein levels across different cell types, tissues, or experimental conditions

    • Immunohistochemistry to examine tissue-specific expression patterns and subcellular localization

    • Immunofluorescence to visualize nuclear speckles where SRSF1 typically concentrates

    • Flow cytometry for analyzing SRSF1 levels at the single-cell level

  • RNA-protein interaction studies:

    • RNA immunoprecipitation (RIP) to identify SRSF1-bound RNA targets

    • CLIP-seq (Cross-linking immunoprecipitation followed by sequencing) to map SRSF1 binding sites on RNAs with nucleotide resolution

    • Research has identified that approximately 41% of mRNAs showing polysomal shifts upon SRSF1 overexpression were previously identified as direct SRSF1 RNA targets by CLIP-seq

  • Splicing regulation analysis:

    • Detection of SRSF1's association with other splicing factors through co-immunoprecipitation

    • Chromatin immunoprecipitation (ChIP) to study SRSF1's association with nascent transcripts

    • Immunodepletion to assess SRSF1's role in in vitro splicing assays

  • Translational control investigation:

    • Polysome profiling combined with SRSF1 detection to study translational regulation

    • Research has demonstrated that SRSF1 activates translation in the cytoplasm and that approximately 1500 mRNAs are translational targets of SRSF1

  • Disease-related research applications:

    • Analysis of SRSF1 expression in cancer tissues to correlate with disease progression

    • Investigation of SRSF1's role in antitumor immunity, as research shows depleting SRSF1 in CD8+ T cells improves antitumor immune function

    • Studying SRSF1 in viral infections, with evidence showing SRSF1 expression is regulated by interferon and impacts HIV-1 replication

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