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The protein encoded by SRSF2 is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Additionally we are shipping SRSF2 Antibodies (34) and SRSF2 Kits (17) and many more products for this protein.
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SRSF2 mutations were significantly related to the shorter OS in patients with myelodysplastic syndromes which may consider as an adverse prognostic risk factor. Whereas, analysis did not show any prognostic effect on overall-survival of chronic myelomonocytic leukemia patients with SRSF2 mutations.
SRSF2 is highly expressed in hepatocellular carcinoma and its expression increases with the degree of tumor differentiation and TNM (show ODZ1 Proteins) staging. It is related to lymph node metastasis and metastasis of tumor cells, and is positively related to serum alpha fetoprotein (show AFP Proteins) content, and affects the postoperative survival time of HCC (show FAM126A Proteins) patients.
We found that SON and SC35 (also known as SRSF2) localize to the central region of the speckle, whereas MALAT1 and small nuclear (sn)RNAs are enriched at the speckle periphery.
Through a serial mutagenesis, authors demonstrate that a 10 nt RNA sequence surrounding the branch-point (BP), is important for SRSF2-mediated inhibition of cassette exon inclusion through directly interacting with SRSF2.
The aberrantly spliced target genes and deregulated cellular pathways associated with the commonly mutated splicing factor (show SLU7 Proteins) genes in myelodysplastic syndromes (SF3B1 (show SF3B2 Proteins), SRSF2 and U2AF1 (show U2AF1 Proteins)) are being identified, illuminating the molecular mechanisms underlying the disease. (Review)
adverse prognostic impact of SRSF2 mutations on OS and AML (show RUNX1 Proteins) transformation in patients with de novo MDS (show PAFAH1B1 Proteins)
SRSF2 mutation is associated with chronic myelomonocytic leukemia.
Mutation in SRSF2 gene is associated with Uveal Melanoma.
Myelodysplastic syndrome -related P95 (show NBN Proteins) point mutants of SRSF2 lead to alternative splicing of CDC25C (show CDC25C Proteins) in a manner that is not dependent on the DNA damage response.
Findings identify SRSF2 as a key regulator of RNA splicing dysregulation in cancer, with possible clinical implications as a candidate prognostic factor in patients with HCC (show FAM126A Proteins).
Mice expressing Srsf2 mutation Srsf2P95H, which commonly occurs in individuals with MDS (show MECOM Proteins) and AML (show RUNX1 Proteins), in an inducible, hemizygous manner in hematopoietic cells rapidly succumbed to fatal bone marrow failure, demonstrating that Srsf2-mutated cells depend on the wild-type Srsf2 allele for survival.
Findings have shown that SRSF2 not only is involved in splicing regulation of a large number of transcripts but also activates transcription of metabolism-related genes and transcription factors.
Depletion of SRSF2 enhances reovirus replication and cytopathic effect, suggesting that T1L (show CERS6 Proteins) mu2 (show AP2M1 Proteins) modulation of splicing benefits the virus.
HIV-1-Tat (show TAT Proteins) Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A (show DYRK1A Proteins) Kinase.
The findings suggest that intact SRSF2 is essential for the functional integrity of the hematopoietic system and that its mutations likely contribute to development of myelodysplastic syndromes.
SRSF2 mutations alter SRSF2's normal sequence-specific RNA binding activity, thereby altering the recognition of specific exonic splicing enhancer motifs to drive recurrent mis (show AMH Proteins)-splicing of key hematopoietic regulators
Study reports that SRSF2 (also known as SC35, an SR-splicing factor (show SLU7 Proteins)) is part of the 7SK complex assembled at gene promoters and plays a direct role in transcription pause release.
Specific effects on regulated splicing by SR proteins SRSF1 (show SRSF1 Proteins) and SRSF2 depends on a complex set of relationships with multiple other SR proteins in mammalian genomes.
Deficiency of the splicing factor (show SLU7 Proteins) Sfrs10 results in early embryonic lethality in mice and has no impact on full-length SMN/Smn (show STMN1 Proteins) splicing.
Oct-4 distribution was examined relative to that of the unphosphorylated form of RNA polymerase II (Pol II) and splicing factor (SC 35) in the intranuclear entities such as perichromatin fibrils.
The protein encoded by this gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation. Two transcript variants encoding the same protein and one non-coding transcript variant have been found for this gene. In addition, a pseudogene of this gene has been found on chromosome 11.
SR splicing factor 2
, splicing component, 35 kDa
, splicing factor SC35
, splicing factor, arginine/serine-rich 2
, myelin regulatory factor 1
, putative myelin regulatory factor 1
, splicing factor Sc35
, splicing factor, arginine/serine-rich 2 (SC-35)
, PR 264 protein
, arginine/serine-rich2 splicing factor