protein

Recombinant Human Heterogeneous nuclear ribonucleoproteins A2/B1

MBS962438

0.05 mg (E-Coli)

180 USD

Recombinant Protein

Recombinant Human Heterogeneous nuclear ribonucleoproteins A2/B1

Heterogeneous nuclear ribonucleoproteins A2/B1

heterogeneous nuclear ribonucleoproteins A2/B1 isoform A2; Heterogeneous nuclear ribonucleoproteins A2/B1; heterogeneous nuclear ribonucleoproteins A2/B1; heterogeneous nuclear ribonucleoprotein A2/B1

HNRNPA2B1

HNRNPA2B1; HNRNPA2B1; RNPA2; HNRPA2; HNRPB1; SNRPB1; HNRNPA2; HNRNPB1; IBMPFD2; HNRPA2B1; HNRPA2B1; hnRNP A2/B1

ROA2_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-249 Full length

249

MEREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCV
VMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRV
VEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLR
DYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDK
IVLQKYHTINGHNAEVRKALSRQEMQEDLEVAILEVAPV
MEEEEEDMVVEDLDMATRVGATEVVMTTMEEEIMEVEIT
MILEIITSNLLTTVQ

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Transcription

Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus.

Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins a diversity of RNA binding proteins is generated by small peptide inserts.Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989) Two homologous genes, originated by duplication, encode the human hnRNP proteins A2 and A1.Biamonti G., Ruggiu M., Saccone S., Della Valle G., Riva S.Nucleic Acids Res. 22:1996-2002(1994) Structure and expression of the gene (HNRPA2B1) encoding the human hnRNP protein A2/B1.Kozu T., Henrich B., Schaefer K.P.Genomics 25:365-371(1995) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Dozynkiewicz M., Norman J.C.Submitted (JUN-2009) to UniProtKB Lubec G., Vishwanath V., Chen W.-Q., Sun Y.Submitted (DEC-2008) to UniProtKB Purification and partial sequencing of the nuclear autoantigen RA33 shows that it is indistinguishable from the A2 protein of the heterogeneous nuclear ribonucleoprotein complex.Steiner G., Hartmuth K., Skriner K., Maurer-Fogy I., Sinski A., Thalmann E., Hassfeld W., Barta A., Smolen J.S.J. Clin. Invest. 90:1061-1066(1992) ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells.Prasad S., Walent J., Dritschilo A.Biochem. Biophys. Res. Commun. 204:772-779(1994) Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins.Kumar A., Willams K.R., Szer W.J. Biol. Chem. 261:11266-11273(1986) Two-dimensional gel electrophoresis, protein electroblotting and microsequencing a direct link between proteins and genes.Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.Electrophoresis 11:528-536(1990) Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.RNA 8:426-439(2002) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.Ong S.E., Mittler G., Mann M.Nat. Methods 1:119-126(2004) Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.J. Proteome Res. 6:4150-4162(2007) Molecular composition of IMP1 ribonucleoprotein granules.Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.Mol. Cell. Proteomics 6:798-811(2007) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(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) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) 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) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) 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) Resveratrol-induced changes of the human adipocyte secretion profile.Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., Mariman E.C., Renes J.J. Proteome Res. 11:4733-4743(2012) 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) C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking.Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., Atkin J.D.Hum. Mol. Genet. 23:3579-3595(2014) 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) Solution structure of RRM domain in heterogeneous nuclear ribonucleoproteins A2/B1.RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bankMutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.Kim H.J., Kim N.C., Wang Y.D., Scarborough E.A., Moore J., Diaz Z., MacLea K.S., Freibaum B., Li S., Molliex A., Kanagaraj A.P., Carter R., Boylan K.B., Wojtas A.M., Rademakers R., Pinkus J.L., Greenberg S.A., Trojanowski J.Q., Traynor B.J., Smith B.N., Topp S., Gkazi A.S., Miller J., Shaw C.E., Kottlors M., Kirschner J., Pestronk A., Li Y.R., Ford A.F., Gitler A.D., Benatar M., King O.D., Kimonis V.E., Ross E.D., Weihl C.C., Shorter J., Taylor J.P.Nature 495:467-473(2013) +Additional computationally mapped references. p>Provides general information on the entry.

4504447

NP_002128.1

NM_002137.3

P22626

55.8kD

Gene Expression Pathway (1269649); Processing Of Capped Intron-Containing Pre-mRNA Pathway (1269688); MRNA Splicing Pathway (1269689); MRNA Splicing - Major Pathway (1269690); MRNA Processing Pathway (198843)

This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. This gene has been described to generate two alternatively spliced transcript variants which encode different isoforms. [provided by RefSeq, Jul 2008]

hnRNP A2/B1: Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Identified in the spliceosome C complex. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with IGF2BP1. 2 isoforms of the human protein are produced by alternative splicing. Protein type: RNA-binding; RNA splicing; Spliceosome. Chromosomal Location of Human Ortholog: 7p15. Cellular Component: cytoplasm; membrane; nucleoplasm; nucleus; ribonucleoprotein complex; spliceosome. Molecular Function: miRNA binding; mRNA 3'-UTR binding; nucleotide binding; protein binding; RNA binding; single-stranded telomeric DNA binding. Biological Process: gene expression; mRNA export from nucleus; mRNA processing; negative regulation of nuclear mRNA splicing, via spliceosome; negative regulation of transcription from RNA polymerase II promoter; nuclear mRNA splicing, via spliceosome; primary microRNA processing; RNA splicing; RNA transport. Disease: Inclusion Body Myopathy With Early-onset Paget Disease With Or Without Frontotemporal Dementia 2

0.05 mg (E-Coli)

180 USD

0.05 mg (Yeast)

260

0.2 mg (E-Coli)

490

0.2 mg (Yeast)

600

0.5 mg (E-Coli)

715