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Validated All-in-One™ qPCR Primer for SRSF1(NM_006924.5) Search again
Product ID:
HQP160711
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ASF, NEDFBA, SF2, SF2p33, SFRS1, SRp30a
Gene Description:
serine and arginine rich splicing factor 1
Target Gene Accession:
NM_006924.5(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins
- encodes for a repressor domain required for its inhibitor activity on pre-mRNA splicing
- acts as a potent regulator of G alpha(s) isoform expression
- SF2/ASF protein inhibits camptothecin-induced DNA cleavage by human topoisomerase I.
- The RNA splicing factor ASF/SF2 inhibits human topoisomerase I mediated DNA relaxation
- ASF/SF2 plays an important role in viral RNA expression and splicing at the proximal 3' splice site.
- c-Src splicing activation by SF2/ASF is dependent on the N1 exon enhancer element. The activity of these exonic splicing regulators, SF2/ASF and hnRNP A1, is linked to the splicing of an exon primarily controlled by intronic factors.
- SR proteins 9G8, SC35, ASF/SF2, and SRp40 have effects on the utilization of the A1 to A5 splicing sites of HIV-1 RNA
- activates the ESE (exon splicing enhancer) which regulates HIV-1 rev, env, vpu, and nef gene expression
- hypophosphorylation of ASF in mRNPs coincides with its higher affinity for TAP
- splicing of beta-tropomyosin exon 6B is repressed by hnRNP A1, and activated by ASF/SF2 and SC35
- SR proteins 9G8 and ASF/SF2 exhibit higher affinity for TAP/NXF1 when hypophosphorylated
- SF2/ASF is part of a complex that forms upon the 79-nucleotide negative regulatory element (NRE) that is thought to be pivotal in posttranscriptional regulation of late gene expression in human papillomavirus type 16
- HIV-2 gag interacts specifically with a serine/throone kinase, PRP4 and down regulates splicing through reduced phosphorylation of SF2.
- SF2 protein is involved in mRNA surveillance.
- SR proteins ASF/SF2, SC35 and 9G8 can down-regulate the late steps of HIV-1 replication via negative impact on RNA splicing and virion production.
- The vivo depletion of ASF/SF2 results in a hypermutation phenotype likely due to DNA rearrangements, reflected in the rapid appearance of DNA double-strand breaks and high-molecular-weight DNA fragments.
- Data suggest that RS-domain phosphorylation may influence the association of splicing factor 2/alternative splicing factor with mRNA, whereas RRM2 may play an important role in mediating protein-protein interactions during translation.
- ASF/SF2 is phosphorylated by SRPK1 and Clk/Sty
- ASF/SF2 inactivation results in a G2-phase cell cycle arrest and subsequent programmed cell death; however, internucleosomal DNA fragmentation is not detected.
- identified SRp30a as an RNA trans-acting factor that functions as a major regulator of caspase-9 pre-mRNA processing and is required for ceramide to mediate the alternative splicing of caspase-9
- In this work we report the identification of a strong SF2/ASF binding site within exon 7 of the human fibrinogen Bbeta-chain gene (FGB).
- Data demonstrate that CDC2L5 is located in the nucleoplasm, where it directly interacts with the ASF/SF2-associated protein p32, a protein involved in splicing regulation.
- Splicing factor SF2/ASF is upregulated in various human tumors, in part due to amplification of its gene, SFRS1.
- a novel role for SR proteins in promoting RSV polyadenylation in the context of the NRS-3' splice site complex, which is thought to bridge the long distance between the NRS and poly(A) site.
- RNPS1 is able to function together with ASF/SF2 to form ribonucleoprotein complexes on nascent transcripts, and thereby prevent formation of transcriptional R-loops.
- These studies reveal that SRPK1 docks near the C-terminus of the RS1 segment of ASF protein and then moves in an N-terminal direction along the RS domain.
- Increased TAP binding correlates with increased SF2/ASF binding, but not increased REF/Aly or Y14 binding.
- ASF/SF2 and SRp55 appear to interact with the variable TF exon 5 through exonic splicing enhancers at bases 39 and 87-117. Weakening of the above ESE modulates splicing of TF exon 5.
- SF2/ASF promotes translation initiation of bound mRNAs; this activity requires the presence of the cytoplasmic cap-binding protein eIF4E.
- poly(ADP-ribose) targeting of topoisomerase I and ASF/SF2 functions may participate in the regulation of gene expression
- Growth hormone deficiency and splicing fidelity: two serine/arginine-rich proteins, ASF/SF2 and SC35, act antagonistically
- Data show that adaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1.
- SF2/ASF splicing factor activates the mTORC1 branch of the pathway
- data presented here indicate that SF2/ASF has the capacity to co-regulate the nuclear and cytoplasmic processing of specific mRNAs and provide further evidence that the nuclear history of an mRNA may influence its cytoplasmic fate
- The authors demonstrate that the HPV16 E2 transcription factor transactivates the SF2/ASF promoter.
- ASF/SF2 and PPAR-gamma determines the ratio of UCP3 isoforms.