Heterogeneous nuclear ribonucleoprotein M Recombinant Protein | HNRNPM recombinant protein

Recombinant Human Heterogeneous nuclear ribonucleoprotein M

Cat. Num. AAA969636

• Gene Names: HNRNPM; CEAR; HNRPM; HTGR1; NAGR1; HNRPM4; HNRNPM4; hnRNP M
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Heterogeneous nuclear ribonucleoprotein M; Recombinant Human Heterogeneous nuclear ribonucleoprotein M; HNRNPM recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-730
• Sequence: AAGVEAAAEVAATEIKMEEESGAPGVPSGNGAPGPKGEGERPAQNEKRKEKNIKRGGNRFEPYANPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKVMATTGGMGMGPGGPGMITIPPSILNNPNIPNEIIHALQAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQSIE
• Sequence Length: 730

• 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 HNRNPM recombinant protein

Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines.

Product Categories/Family for HNRNPM recombinant protein

Epigenetics and Nuclear Signaling

References

The human hnRNP M proteins identification of a methionine/arginine-rich repeat motif in ribonucleoproteins.Datar K.V., Dreyfuss G., Swanson M.S.Nucleic Acids Res. 21:439-446(1993) The human hnRNP-M proteins structure and relation with early heat shock-induced splicing arrest and chromosome mapping.Gattoni R., Mahe D., Mahl P., Fischer N., Mattei M.-G., Stevenin J., Fuchs J.-P.Nucleic Acids Res. 24:2535-2542(1996) A new human M4 protein with deletion.Zhao Z., Huang X., Li N., Cao X. Bienvenut W.V.Submitted (OCT-2004) to UniProtKB 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) Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates.Gocke C.B., Yu H., Kang J.J. Biol. Chem. 280:5004-5012(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) 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) 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) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(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) Solution structure of the RNA binding domains of heterogeneous nuclear ribonucleoprotein M.RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 14141152
• NCBI GeneID: 4670
• NCBI Accession #: NP_005959.2
• NCBI GenBank Nucleotide #: NM_005968.4
• UniProt Accession #: P52272; Q15584; Q8WZ44; Q96H56; Q9BWL9; Q9Y492
• Molecular Weight: 93.33kD
• NCBI Official Full Name: heterogeneous nuclear ribonucleoprotein M isoform a
• NCBI Official Synonym Full Names: heterogeneous nuclear ribonucleoprotein M
• NCBI Official Symbol: HNRNPM
• NCBI Official Synonym Symbols: CEAR; HNRPM; HTGR1; NAGR1; HNRPM4; HNRNPM4; hnRNP M
• NCBI Protein Information: heterogeneous nuclear ribonucleoprotein M
• UniProt Protein Name: Heterogeneous nuclear ribonucleoprotein M
• Protein Family: Heterogeneous nuclear ribonucleoprotein
• UniProt Gene Name: HNRNPM
• UniProt Synonym Gene Names: HNRPM; NAGR1; hnRNP M
• UniProt Entry Name: HNRPM_HUMAN

NCBI Description

This gene belongs to the 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 three repeats of quasi-RRM domains that bind to RNAs. This protein also constitutes a monomer of the N-acetylglucosamine-specific receptor which is postulated to trigger selective recycling of immature GlcNAc-bearing thyroglobulin molecules. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2011]

Uniprot Description

hnRNP M: Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Receptor, misc.; Nucleolus; RNA splicing; RNA-binding; Spliceosome

Chromosomal Location of Human Ortholog: 19p13.2

Cellular Component: cell surface; extracellular matrix; integral to plasma membrane; membrane; nuclear matrix; nucleolus; nucleoplasm; paraspeckles; spliceosome

Molecular Function: calcium-dependent protein binding; nucleotide binding; protein binding; protein domain specific binding; RNA binding

Biological Process: alternative nuclear mRNA splicing, via spliceosome; gene expression; nuclear mRNA splicing, via spliceosome; RNA splicing