Recombinant Human RNA-binding protein FUS | MyBioSource MBS717142 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human RNA-binding protein FUS

catalog :

MBS717142

quantity :

0.05 mg (E-Coli)

price :

180 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS717142

products type :

Recombinant Protein

products full name :

Recombinant Human RNA-binding protein FUS

products short name :

RNA-binding protein FUS

products name syn :

75 kDa DNA-pairing protein; Oncogene FUS; Oncogene TLSPOMp75; Translocated in liposarcoma protein

other names :

RNA-binding protein FUS isoform 2; RNA-binding protein FUS; RNA-binding protein FUS; FUS RNA binding protein; 75 kDa DNA-pairing protein; Oncogene FUS; Oncogene TLS; POMp75; Translocated in liposarcoma protein

products gene name :

FUS

products gene name syn :

TLS

other gene names :

FUS; FUS; TLS; ALS6; ETM4; FUS1; POMP75; HNRNPP2; TLS

uniprot entry name :

FUS_HUMAN

host :

E Coli

sequence positions :

1-198; Partial.

sequence length :

198

sequence :

MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYS
GYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGST
GGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSS
QSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYG
QQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYG
NQD

purity :

Greater than 90% as determined by SDS-PAGE.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Epigenetics and Nuclear Signaling

products description :

Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complentary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.

products references :

Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma.Crozat A., Aman P., Mandahl N., Ron D.Nature 363:640-644(1993) Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma.Rabbitts T.H., Forster A., Larson R., Nathan P.Nat. Genet. 4:175-180(1993) Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes.Morohoshi F., Ootsuka Y., Arai K., Ichikawa H., Mitani S., Munakata N., Ohki M.Gene 221:191-198(1998) The sequence and analysis of duplication-rich human chromosome 16.Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.Nature 432:988-994(2004) Genetic characterization of angiomatoid fibrous histiocytoma identifies fusion of the FUS and ATF-1 genes induced by a chromosomal translocation involving bands 12q13 and 16p11.Waters B.L., Panagopoulos I., Allen E.F.Cancer Genet. Cytogenet. 121:109-116(2000) Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation.Baechtold H., Kuroda M., Sok J., Ron D., Lopez B.S., Akhmedov A.T.J. Biol. Chem. 274:34337-34342(1999) Human POMp75 is identified as the pro-oncoprotein TLF/FUS both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation.Bertrand P., Akhmedov A.T., Delacote F., Durrbach A., Lopez B.S.Oncogene 18:4515-4521(1999) Lubec G., Chen W.-Q., Sun Y.Submitted (DEC-2008) to UniProtKB An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation.Ichikawa H., Shimizu K., Hayashi Y., Ohki M.Cancer Res. 54:2865-2868(1994) The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription.Zhang D., Paley A.J., Childs G.J. Biol. Chem. 273:18086-18091(1998) Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing.Yang L., Embree L.J., Tsai S., Hickstein D.D.J. Biol. Chem. 273:27761-27764(1998) Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode.Rappsilber J., Friesen W.J., Paushkin S., Dreyfuss G., Mann M.Anal. Chem. 75:3107-3114(2003) Intracellular characterization of DDX39, a novel growth-associated RNA helicase.Sugiura T., Sakurai K., Nagano Y.Exp. Cell Res. 313:782-790(2007) TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules.Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.Hum. Mol. Genet. 17:3055-3074(2008) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) 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) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) 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) Northeast structural genomics consortium target HR6430A.Northeast structural genomics consortium (NESG) Submitted (MAY-2011) to the PDB data bankThe consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis.Kwiatkowski T.J. Jr., Bosco D.A., Leclerc A.L., Tamrazian E., Vanderburg C.R., Russ C., Davis A., Gilchrist J., Kasarskis E.J., Munsat T., Valdmanis P., Rouleau G.A., Hosler B.A., Cortelli P., de Jong P.J., Yoshinaga Y., Haines J.L., Pericak-Vance M.A., Yan J., Ticozzi N., Siddique T., McKenna-Yasek D., Sapp P.C., Horvitz H.R., Landers J.E., Brown R.H. Jr.Science 323:1205-1208(2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6.Vance C., Rogelj B., Hortobagyi T., De Vos K.J., Nishimura A.L., Sreedharan J., Hu X., Smith B., Ruddy D., Wright P., Ganesalingam J., Williams K.L., Tripathi V., Al-Saraj S., Al-Chalabi A., Leigh P.N., Blair I.P., Nicholson G., de Belleroche J., Gallo J.M., Miller C.C., Shaw C.E.Science 323:1208-1211(2009) Mutations of FUS gene in sporadic amyotrophic lateral sclerosis.Corrado L., Del Bo R., Castellotti B., Ratti A., Cereda C., Penco S., Soraru G., Carlomagno Y., Ghezzi S., Pensato V., Colombrita C., Gagliardi S., Cozzi L., Orsetti V., Mancuso M., Siciliano G., Mazzini L., Comi G.P., Gellera C., Ceroni M., D'Alfonso S., Silani V.J. Med. Genet. 47:190-194(2010) Genetic contribution of FUS to frontotemporal lobar degeneration.Van Langenhove T., van der Zee J., Sleegers K., Engelborghs S., Vandenberghe R., Gijselinck I., Van den Broeck M., Mattheijssens M., Peeters K., De Deyn P.P., Cruts M., Van Broeckhoven C.Neurology 74:366-371(2010) Exome sequencing identifies fus mutations as a cause of essential tremor.Merner N.D., Girard S.L., Catoire H., Bourassa C.V., Belzil V.V., Riviere J.B., Hince P., Levert A., Dionne-Laporte A., Spiegelman D., Noreau A., Diab S., Szuto A., Fournier H., Raelson J., Belouchi M., Panisset M., Cossette P., Dupre N., Bernard G., Chouinard S., Dion P.A., Rouleau G.A.Am. J. Hum. Genet. 91:313-319(2012)

ncbi gi num :

283135201

ncbi acc num :

NP_001164105.1

ncbi gb acc num :

NM_001170634.1

uniprot acc num :

P35637

ncbi mol weight :

47.5kD

ncbi pathways :

Gene Expression Pathway (1269649); Processing Of Capped Intron-Containing Pre-mRNA Pathway (1269688); Transcriptional Misregulation In Cancer Pathway (523016); Transcriptional Misregulation In Cancer Pathway (522987); MRNA Splicing Pathway (1269689); MRNA Splicing - Major Pathway (1269690); MRNA Processing Pathway (198843)

ncbi summary :

This gene encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The hnRNP complex is involved in pre-mRNA splicing and the export of fully processed mRNA to the cytoplasm. This protein belongs to the FET family of RNA-binding proteins which have been implicated in cellular processes that include regulation of gene expression, maintenance of genomic integrity and mRNA/microRNA processing. Alternative splicing results in multiple transcript variants. Defects in this gene result in amyotrophic lateral sclerosis type 6. [provided by RefSeq, Sep 2009]

uniprot summary :

hnRNP P2: Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single- stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity. Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-terminus with SFRS13A. Interacts with OTUB1 and SARNP. Ubiquitous. Belongs to the RRM TET family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: DNA-binding; Nuclear receptor co-regulator; RNA-binding; RNA splicing; Oncoprotein. Chromosomal Location of Human Ortholog: 16p11.2. Cellular Component: nucleoplasm; nucleus; perikaryon; perinuclear region of cytoplasm; polysome. Molecular Function: DNA binding; estrogen receptor binding; identical protein binding; ionotropic glutamate receptor binding; myosin V binding; nucleotide binding; protein binding; retinoid X receptor binding; RNA binding; thyroid hormone receptor binding; transcription coactivator activity; zinc ion binding. Biological Process: gene expression; nuclear mRNA splicing, via spliceosome; RNA splicing. Disease: Amyotrophic Lateral Sclerosis 6, With Or Without Frontotemporal Dementia; Tremor, Hereditary Essential, 4

size1 :

0.05 mg (E-Coli)

price1 :

180 USD

size2 :

0.2 mg (E-Coli)

price2 :

490

size3 :

0.5 mg (E-Coli)

price3 :

715

size4 :

1 mg (E-Coli)

price4 :

1170

more info or order :

MyBioSource product webpage