Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human SRSF1 Antikörper:
anti-Mouse (Murine) SRSF1 Antikörper:
anti-Rat (Rattus) SRSF1 Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Human Polyclonal SRSF1 Primary Antibody für ICC, IF - ABIN4353084
Brown, Dobrikov, Gromeier et al.: Mitogen-activated protein kinase-interacting kinase regulates mTOR/AKT signaling and controls the serine/arginine-rich protein kinase-responsive type 1 internal ribosome entry site-mediated ... in Journal of virology 2014
Show all 2 Pubmed References
Cow (Bovine) Polyclonal SRSF1 Primary Antibody für IHC, WB - ABIN2779013
Velazquez-Dones, Hagopian, Ma, Zhong, Zhou, Ghosh, Fu, Adams: Mass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty. in The Journal of biological chemistry 2005
Show all 2 Pubmed References
SRSF1 expression levels were significantly lower in T cells from systemic lupus erythematosus (SLE) patients compared to healthy subjects, and correlated inversely with disease activity and positively with levels of RasGRP1-WT and DNMT1. AS to RasGRP1-WT and decreased levels of RasGRP1 protein, whereas overexpression of SRSF1 in SLE T-cells caused recovery of RasGRP1, which in turn induced DNMT1/interleukin-2 expression.
LIG1 is regulated by the oncoprotein SRSF1 and plays a relevant role in lung cancer cell proliferation and progression.
Interaction and kinetic assays unveiled how SRSF1 and the single RRM-containing SRSF3 are phosphorylated by SRPK2, another member of the SRPK family.
SRSF1 regulates lung cancer cell radioresistance through modulating PTPMT1 splicing. Reduced SRSF1 favors the production of short isoforms of PTPMT1 upon ionizing radiation, which in turn promotes phosphorylation of AMPK, thereby inducing DNA double-strand break to sensitize cancer cells to irradiation.
Results identify for the first time that the phosphorylation state of SRSF1 is linked to different phases in pediatric ALL. The Tyr-19 phosphorylation of SRSF1 disrupts its subcellular localization and promotes proliferation in leukemia cells by driving cell-cycle progression.
SRSF1 promotes vascular smooth muscle cell (VSMC) proliferation and injury-induced neointima formation. SRSF1 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, resulting in an accelerated cell-cycle progression and increased VSMC proliferation.
repeat RNA-sequestration of SRSF1 triggers the NXF1-dependent nuclear export of C9ORF72 transcripts retaining expanded hexanucleotide repeats
A -44 G to A "hot zone" putative functional noncoding variant of SRSF1 was found in an AML patient. It alters the binding activities of E2F6, ELF1, and ELK4, ELK4.
We now show that the ability of SRPK1 to mobilize SRSF1 from speckles to the nucleoplasm is dependent on active CLK1. Diffusion from speckles is promoted by the formation of an SRPK1-CLK1 complex that facilitates dissociation of SRSF1 from CLK1 and enhances the phosphorylation of several serine-proline dipeptides in this SR protein
Authors showed that Mir505-3p was capable of inhibiting tumor proliferation driven by SRSF1 in two neural tumor cell lines, Neuro-2a (N2a) and U251, exclusively in serum-reduced condition. Authors observed that the protein level of SRSF1 was gradually promoted by increasing concentration of serum.
The present study suggested that the tumor suppressor miR30c may be involved in prostate cancer tumorigenesis, possibly via targeting ASF/SF2.
It has been proposed that SF2/ASF has a protective role against JC virus reactivation in multiple sclerosis patients.
Immune suppression of JC virus gene expression is mediated by SRSF1.
ASF/SF2 is identified as a splicing regulator of cyclin T1, which contributes to the control of the subsequent transcription events.
Findings suggest MALAT1 increases AKAP-9 expression by promoting SRPK1-catalyzed SRSF1 phosphorylation in CRC cells. These results reveal a novel molecular mechanism by which MALAT1 regulates AKAP-9 expression in CRC cells.
high level of SF2, as a novel oncoprotein in RCC, was significantly associated with poor survival in a large cohort of RCC specimens. Taken together, our study presents a road map for the prediction and validation of miR-766-3p/SF2 axis and thus imparts a therapeutic way for further RCC progression.
The authors found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism.
We present a joint atomistic molecular dynamics (MD) and experimental study of two RRM-containing proteins bound with their single-stranded target RNAs, namely the Fox-1 and SRSF1 complexes.The simulations predict unanticipated specific participation of Arg142 at the protein-RNA interface of the SRFS1 complex, which is subsequently confirmed by NMR and ITC measurements
Using NMR spectroscopy with two separately expressed domains of SRSF1, we showed that several residues in the RNA-binding motif 2 interact with the N-terminal region of the RS domain (RS1).
Especially, in SRSF1 morphants, bone cartilage formation was reduced in the brain and Nkx-2.5 expression was dramatically reduced in the heart of SRSF1 morphants. In addition, a dramatic reduction in functional chordin RNA in SRSF1 morphants was observed suggesting that chordin is one of the targets of SRSF1. Thus, we concluded that SRSF1 is an essential factor for pattern formation including heart, cartilage and germ lay
In addition, overexpression of SRSF1 in XRCC4-deficient cells restored the normal level of apoptosis, suggesting that SRSF1 functions downstream of XRCC4 in activating CAD.
SRSF1 is a key regulator of DBF4B pre-mRNA splicing dysregulation in colon cancer. SRSF1 is required for cancer cell proliferation.
LncRNA MALAT1 is dysregulated in diabetic nephropathy and involved in high glucose-induced podocyte injury via its interplay with beta-catenin and SRSF1.
This study showed that the splicing factor kinase SRPK1 is a key regulator of spinal nociceptive processing in naive and nerve injured animals. We present evidence for a novel mechanism in which altered SRSF1 localization/function in neuropathic pain results in sensitization of spinal cord neurons.
The expression levels of three splicing factors, ESRP1, PTB and SF2/ASF, are significantly altered during cardiac hypertrophy in mice.
RRP1B suppresses metastatic progression by altering the transcriptome through its interaction with splicing regulators such as SRSF1
Deletion of RRM1 eliminated the splicing activity of SRSF1 and thus cellular transformation.
Specific effects on regulated splicing by SR proteins SRSF1 and SRSF2 depends on a complex set of relationships with multiple other SR proteins in mammalian genomes.
Treatment with IL-17 prolongs the half-life of chemokine CXCL1 mRNA via the adaptor TRAF5 and the splicing-regulatory factor SF2 (ASF).
analysis of the miRNA-mediated interaction between leukemia/lymphoma-related factor (LRF) and alternative splicing factor/splicing factor 2 (ASF/SF2) affects cell senescence and apoptosis
Modulation of Xist RNA processing may be part of the stochastic process that determines which X chromosome will be inactivated.
Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1
Both hnRNP A1 and alternative splicing factor/splicing factor 2 contents rose in adenomas and during injury-induced hyperplasia compared to control lungs
These results highlight the requirement of Sfrs1-mediated alternative splicing for the survival of retinal neurons, with sensitivity defined by the window of time in which the neuron was generated.
This gene encodes 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. In addition, a pseudogene of this gene has been found on chromosome 13.
, SR splicing factor 1
, alternative-splicing factor 1
, pre-mRNA-splicing factor SF2, P33 subunit
, splicing factor 2
, splicing factor, arginine/serine-rich 1
, pre-mRNA-splicing factor SRp30a
, splicing factor, arginine/serine-rich 1 (ASF/SF2)
, splicing factor, arginine/serine-rich 1 (splicing factor 2, alternate splicing factor)
, splicing factor, arginine/serine-rich 1B
, splicing factor arginine/serine-rich 1
, serine/arginine-rich splicing factor 1B
, splicing factor, arginine/serine-rich 1b