03-100 RIPAb+™ hnRNP M1-M4

03-100
10 assays  10 assays per set. Recommended use: ~5 μg of antibody per RIP (dependent upon biological context).
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      Overview

      Replacement Information

      Key Specifications Table

      Species ReactivityKey Applications
      B, H, M, Po, R, Rb RIP, WB
      Description
      Catalogue Number03-100
      Trade Name
      • RIPAb+
      • Upstate
      DescriptionRIPAb+™ hnRNP M1-M4
      OverviewRIPAb+ antibodies are evaluated using the RNA Binding Protein Immunoprecipitation (RIP) assay. Each RIPAb+ antibody set includes a negative control antibody to ensure specificity of the RIP reaction and is verified for the co-immunoprecipitation of RNA associated specifically with the immunoprecipitated RNA binding protein of interest. Where appropriate, the RIPAb+ set also includes quantitative RT-PCR control primers (RIP Primers) to biologically validate your IP results by successfully co-precipitating the specific RNA targets, such as messenger RNAs. The qPCR protocol and primer sequences are provided, allowing researchers to validate RIP protocols when using the antibody in their experimental context. If a target specific assay is not provided, the RIPAb+ kit is validated using an automated microfluidics-based assay by enrichment of detectable RNA over control immunoprecipitation.
      The hnRNP M1-M4 proteins are pre-mRNA-binding proteins that complex with heterogeneous nuclear RNA (hnRNA). These proteins associate with pre-mRNAs in the nucleus and influence pre-mRNA processing and other aspects of mRNA metabolism and transport.
      Background InformationPolycomb group proteins are important for maintaining transcriptional silencing. One conserved PcG complex, PRC2, is composed of several proteins including the histone methyltransferase EZH2, the WD-repeat protein EED (Embryonic ectoderm development), and the Zn-finger protein Suz12. Transcriptional repression mediated by EED involves histone deacetylation, while the EZH2 methylates histone H3 on lysine 27. EED protein is present in four isoforms. These EED isoforms selectively associate with distinct EZH2-containing complexes, resulting in differential targeting of their associated methyltransferase activity. These complexes play a role in Hox gene silencing, X-inactivation, germline development, stem cell pluripotency and cancer metastasis.
      References
      Product Information
      FormatPurified
      Control
      • Includes negative control normal mouse IgG antibody and control primers specific for the cDNA of human hnRNP M.
      PresentationAnti-hnRNP M1-M4 (Mouse Monoclonal), Part # CS207316. One vial containing 50 μg of protein G purified mouse IgG1 in 0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide and 30% glycerol. Store at -20°C.
      Normal Mouse IgG, Part # CS200621. One vial containing 125 µg of purified mouse IgG in 125 µL of storage buffer containing 0.1% sodium azide. Store at -20°C.
      RIP Primers, hnRNP M, Part # CS207306. One vial containing 75 μL of 5 μM of each primer specific for human hnRNP M mRNA. Store at -20°C.
      FOR: GAG GCC ATG CTC CTG GG
      REV: TTT AGC ATC TTC CAT GTG AAA TCG
      Applications
      Key Applications
      • RNA Binding Protein Immunoprecipitation (RIP)
      • Western Blotting
      Application NotesImmunoprecipitation from RIP lysate:
      Representative lot data.
      RIP lysate from HeLa cells (~2 X 10E7 cell equivalents per IP) was subjected to immunoprecipitation using 5 µg of either a normal mouse IgG, (Cat. # CS200621), or 5 µg of Anti-hnRNP M1-M4 antibody (Cat. # CS207316). Ten percent of the precipitated proteins (lane 1: normal mouse IgG, lane 2: hnRNP M1-M4) were resolved by electrophoresis, transferred to nitrocellulose and probed with anti-hnRNP M1-M4 (Cat. # CS207316, 1:1000). Proteins were visualized using One-Step™ IP-Western kit (GenScript Cat. # L00231).
      Arrow indicates hnRNP M1-M4. (Figure 2).
      Automated Microfluidics-based Electrophoretic RNA Separation and Analysis (MFE):
      Representative lot data.
      RIP Lysate prepared from HeLa cells (2 X 10E7 cell equivalents per IP) were subjected to immunoprecipitation using 5 µg of either 1. normal mouse IgG (Cat. # CS200621), or 2. Anti-hnRNP M1-M4 antibody (Cat. # CS207316) and the Magna RIP™ RNA-Binding Protein Immunoprecipitation Kit (Cat. # 17-700).
      Successful immunoprecipitation of hnRNP M1-M4-associated RNA was verified by automated microfluidics-based electrophoretic RNA separation and analysis. Please refer to the Magna RIP™ (Cat. # 17-700) or EZ-Magna RIP™ (Cat. # 17-701) protocol for experimental details. Electropherograms were generated by plotting fluorescence intensities versus migration times (Figure 3A). The virtual gel view was created from this data (Figure 3B).
      Western Blot Analysis:
      Representative lot data.
      HeLa nuclear extract was resolved by electrophoresis, transferred to PVDF and probed with anti-hnRNP M1-M4 (2 µg/mL). Proteins were visualized using a goat anti-mouse IgG secondary antibody conjugated to HRP and a chemiluminescence detection system.
      Arrow indicates hnRNP M1-M4. (Figure 4).
      Biological Information
      ImmunogenT7 gene 10 fusion protein containing full length human RNP M4
      Concentration0.7 mg/mL
      HostMouse
      SpecificityThis antibody recognizes hnRNP M1-M4.
      IsotypeIgG1
      Species Reactivity
      • Bovine
      • Human
      • Mouse
      • Pig
      • Rat
      • Rabbit
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryThis 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 and also contains a nuclear localization motif. Multiple alternatively spliced transcript variants have been found for this gene.
      Gene Symbol
      • HNRPR
      • hnRNP-R
      • FLJ25714
      • HNRNP-R
      • HNRNPR
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: O43390 # Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.
      SIZE: 633 amino acids; 70943 Da
      SUBUNIT: Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRNPA1, HNRNPA2B1, HNRPA3, HNRNPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRNPR, HNRNPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
      SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
      SIMILARITY: SwissProt: O43390 ## Contains 3 RRM (RNA recognition motif) domains.
      Molecular Weight64-68kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceRNA Binding Protein Immunoprecipitation:
      Representative lot data.
      RIP Lysate prepared from HeLa cells (2 X 10E7 cell equivalents per IP) were subjected to immunoprecipitation using 5 µg of either a normal mouse IgG or 5 µg of Anti-hnRNP M1-M4 antibody and the Magna RIP™ RNA-Binding Protein Immunoprecipitation Kit (Cat. # 17-700).
      Successful immunoprecipitation of hnRNP M1-M4-associated RNA was verified by qPCR using RIP Primers hnRNP M, (Figure 1).
      Please refer to the Magna RIP™ (Cat. # 17-700) or EZ-Magna RIP™ (Cat. # 17-701) protocol for experimental details.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable for 1 year at -20°C from date of receipt.
      Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variabillity in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
      Packaging Information
      Material Size10 assays
      Material Package10 assays per set. Recommended use: ~5 μg of antibody per RIP (dependent upon biological context).
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      SDS

      Title

      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      RIPAb+ hnRNP M1-M4 - NRG1880396NRG1880396
      RIPAb+™ hnRNP M1-M4 - 25640332564033
      RIPAb+™ hnRNP M1-M4 -25965182596518
      RIPAb+™ hnRNP M1-M4 -27672162767216

      References

      Reference overviewApplicationPub Med ID
      RNA-binding proteins regulate the expression of the immune activating ligand MICB.
      Nachmani, D; Gutschner, T; Reches, A; Diederichs, S; Mandelboim, O
      Nature communications  5  4186  2014

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      Synaptoneurosome micromethod for fractionation of mouse and human brain, and primary neuronal cultures.
      Julia W Chang,Monica M Arnold,Anna Rozenbaum,Anna Caputo,Felix E Schweizer,My Huynh,Gary W Mathern,Theodore A Sarafian,Joseph B Watson
      Journal of neuroscience methods  211  2012

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      23017979 23017979
      Upregulation of presynaptic mGluR2, but not mGluR3 in the epileptic medial perforant path.
      Judith Rohde,Timo Kirschstein,Wiebke Wilkars,Lorenz Müller,Tursonjan Tokay,Katrin Porath,Roland A Bender,Rüdiger Köhling
      Neuropharmacology  62  2012

      Show Abstract
      22202905 22202905
      Onset coding is degraded in auditory nerve fibers from mutant mice lacking synaptic ribbons.
      Bradley N Buran,Nicola Strenzke,Andreas Neef,Eckart D Gundelfinger,Tobias Moser,M Charles Liberman
      The Journal of neuroscience : the official journal of the Society for Neuroscience  30  2010

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      Fluorescence-activated cell sorting in plant developmental biology.
      Anjali S Iyer-Pascuzzi,Philip N Benfey
      Methods in molecular biology (Clifton, N.J.)  655  2010

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      Paraquat toxicity induced by voltage-dependent anion channel 1 acts as an NADH-dependent oxidoreductase.
      Hiroki Shimada,Kei-Ichi Hirai,Eriko Simamura,Toshihisa Hatta,Hiroki Iwakiri,Keiji Mizuki,Taizo Hatta,Tatsuya Sawasaki,Satoko Matsunaga,Yaeta Endo,Shigeomi Shimizu
      The Journal of biological chemistry  284  2009

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      Loss of synaptophysin-positive boutons on lumbar motor neurons innervating the medial gastrocnemius muscle of the SOD1G93A G1H transgenic mouse model of ALS.
      Da Wei Zang,Elizabeth C Lopes,Surindar S Cheema
      Journal of neuroscience research  79  2005

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      Proline-glutamate interactions in the CNS.
      J G Ortiz,M L Cordero,A Rosado
      Progress in neuro-psychopharmacology & biological psychiatry  21  1997

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      3,5-Di-iodo-L-thyronine suppresses TSH in rats in vivo and in rat pituitary fragments in vitro.
      C Horst,A Harneit,H J Seitz,H Rokos
      The Journal of endocrinology  145  1995

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      Chick sympathetic neurons in culture respond differentially to nerve growth factor and conditioned medium from activated splenic lymphocytes.
      J J Luo,S Hasegawa
      Neuroscience research  10  1991

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      Brochure

      Title
      New Products: Volume 3, 2012