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Heterogeneous Nuclear Ribonucleoproteins A2/B1 (HNRNPA2B1) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS962438

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

$330 / 0.02 mg (Yeast) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Heterogeneous nuclear ribonucleoproteins A2/B1 (HNRNPA2B1), Recombinant Protein
Full Product Name
Recombinant Human Heterogeneous nuclear ribonucleoproteins A2/B1
Sequence
MEREKEQFRK LFIGGLSFET TEESLRNYYE QWGKLTDCVV MRDPASKRSR GFGFVTFSSM AEVDAAMAAR PHSIDGRVVE PKRAVAREES GKPGAHVTVK KLFVGGIKED TEEHHLRDYF EEYGKIDTIE IITDRQSGKK RGFGFVTFDD HDPVDKIVLQ KYHTINGHNA EVRKALSRQE MQEDLEVAIL EVAPVMEEEE EDMVVEDLDM ATRVGATEVV MTTMEEEIME VEITMILEII TSNLLTTVQ
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
30.4 kDa
Sequence Positions
1-249aa; Full Length
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
600124
3D Structure
ModBase 3D Structure for P22626
Production Note
Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to support@mybiosource.com for more details.

Product Categories/Family for HNRNPA2B1 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for HNRNPA2B1 recombinant protein

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.

Other Notes

Small volumes of HNRNPA2B1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for HNRNPA2B1 purchase

MBS962438 is a recombinant protein targeting HNRNPA2B1. Also known as Recombinant Human Heterogeneous nuclear ribonucleoproteins A2/B1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for HNRNPA2B1. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
heterogeneous nuclear ribonucleoproteins A2/B1 isoform A2
NCBI Official Synonym Full Names
heterogeneous nuclear ribonucleoprotein A2/B1
NCBI Official Symbol
HNRNPA2B1
NCBI Official Synonym Symbols
RNPA2; HNRPA2; HNRPB1; SNRPB1; HNRNPA2; HNRNPB1; IBMPFD2; HNRPA2B1
UniProt Protein Name
Heterogeneous nuclear ribonucleoproteins A2/B1
UniProt Gene Name
HNRNPA2B1
UniProt Synonym Gene Names
HNRPA2B1; hnRNP A2/B1
UniProt Entry Name
ROA2_HUMAN
NCBI Protein Information
heterogeneous nuclear ribonucleoproteins A2/B1

NCBI Summary for HNRNPA2B1

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]
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UniProt Comments for HNRNPA2B1

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
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

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