Serine/arginine-rich splicing factor 9 Recombinant Protein | SFRS9 recombinant protein

Recombinant Human Serine/arginine-rich splicing factor 9

Cat. Num. AAA717157

• Gene Names: SRSF9; SFRS9; SRp30c
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Serine/arginine-rich splicing factor 9; Recombinant Human Serine/arginine-rich splicing factor 9; Pre-mRNA-splicing factor SRp30C; Splicing factor; arginine/serine-rich 9; SFRS9 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-221aa; Full Length
• Sequence: MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
• Sequence Length: 221

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for SFRS9 recombinant protein

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10

Product Categories/Family for SFRS9 recombinant protein

Transcription

References

Identification and characterization of three members of the human SR family of pre-mRNA splicing factors.Screaton G.R., Caceres J.F., Mayeda A., Bell M.V., Plebanski M., Jackson D.G., Bell J.I., Krainer A.R.EMBO J. 14:4336-4349(1995) Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12.Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.The finished DNA sequence of human chromosome 12.Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) PIR1, a novel phosphatase that exhibits high affinity to RNA ribonucleoprotein complexes.Yuan Y., Li D.-M., Sun H.J. Biol. Chem. 273:20347-20353(1998) SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements.Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L., Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.Nucleic Acids Res. 26:3542-3549(1998) The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation.Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A., Russell W.C., Akusjarvi G.EMBO J. 18:1014-1024(1999) Alternative splicing determines the intracellular localization of the novel nuclear protein Nop30 and its interaction with the splicing factor SRp30c.Stoss O., Schwaiger F.-W., Cooper T.A., Stamm S.J. Biol. Chem. 274:10951-10962(1999) Stress-induced nuclear bodies are sites of accumulation of pre-mRNA processing factors.Denegri M., Chiodi I., Corioni M., Cobianchi F., Riva S., Biamonti G.Mol. Biol. Cell 12:3502-3514(2001) SRp30c-dependent stimulation of survival motor neuron (SMN) exon 7 inclusion is facilitated by a direct interaction with hTra2 beta 1.Young P.J., DiDonato C.J., Hu D., Kothary R., Androphy E.J., Lorson C.L.Hum. Mol. Genet. 11:577-587(2002) SRp30c is a repressor of 3' splice site utilization.Simard M.J., Chabot B.Mol. Cell. Biol. 22:4001-4010(2002) Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection.Raffetseder U., Frye B., Rauen T., Juerchott K., Royer H.-D., Jansen P.L., Mertens P.R.J. Biol. Chem. 278:18241-18248(2003) Tra2 beta, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA.Kondo S., Yamamoto N., Murakami T., Okumura M., Mayeda A., Imaizumi K.Genes Cells 9:121-130(2004) Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors.Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.J. Neurochem. 88:1078-1090(2004) Tau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c SRp55 complex that either recruits or antagonizes htra2beta1.Wang Y., Wang J., Gao L., Lafyatis R., Stamm S., Andreadis A.J. Biol. Chem. 280:14230-14239(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.J. Proteome Res. 7:5167-5176(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)

NCBI and Uniprot Product Information

• NCBI GI #: 4506903
• NCBI GeneID: 8683
• NCBI Accession #: NP_003760.1
• NCBI GenBank Nucleotide #: NM_003769.2
• UniProt Accession #: Q13242; Q52LD1
• Molecular Weight: 52.5 kDa
• NCBI Official Full Name: serine/arginine-rich splicing factor 9
• NCBI Official Synonym Full Names: serine/arginine-rich splicing factor 9
• NCBI Official Symbol: SRSF9
• NCBI Official Synonym Symbols: SFRS9; SRp30c
• NCBI Protein Information: serine/arginine-rich splicing factor 9
• UniProt Protein Name: Serine/arginine-rich splicing factor 9
• Protein Family: Serine/arginine-rich splicing factor
• UniProt Gene Name: SRSF9
• UniProt Synonym Gene Names: SFRS9; SRP30C
• UniProt Entry Name: SRSF9_HUMAN

NCBI Description

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 pseudogenes, one on chromosome 15 and the other on chromosome 21, have been found for this gene. [provided by RefSeq, Sep 2010]

Uniprot Description

SFRS9: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. Belongs to the splicing factor SR family.

Protein type: RNA splicing; RNA-binding; Spliceosome

Chromosomal Location of Human Ortholog: 12q24.31

Cellular Component: nucleolus; nucleoplasm

Molecular Function: nucleotide binding; protein binding

Biological Process: gene expression; mRNA 3'-end processing; mRNA export from nucleus; mRNA processing; mRNA splice site selection; negative regulation of nuclear mRNA splicing, via spliceosome; nuclear mRNA splicing, via spliceosome; RNA splicing; termination of RNA polymerase II transcription; transcription from RNA polymerase II promoter