RIP-Assay Kit

  • Target RNP Complex
  • Code # RN1001
  • Size 10 Assays
  • Price
    $243.34
Specifications

Background

Post-transcriptional regulation of gene expression is a ribonucleoprotein (RNP)-driven process, which involves RNA binding proteins (RBPs) and noncoding RNAs that regulate splicing, nuclear export, subcellular localization, mRNA stability and translation. This area has recently become the focus of many research groups and progress is being made using the yeast, Saccharomyces cerevisiae and various types of mammalian cell systems. Those observations have confirmed the posttranscriptional RNA operon concept in which mRNAs that encode functionally related proteins are coordinately regulated during cellular processes such as proliferation, differentiation or drug treatment. For example, mRNAs encoding proteins that function in a particular cell process or pathway can be found within a unique mRNP complex, which consists of mRNA and RNP. This provides valuable information regarding not only known components of a particular process or pathway, but importantly, leads to the identification of novel components representing potential therapeutic targets and biomarkers. In addition to those targets identified by pathway expansion, the specific RBPs regulating RNA functions may be potential therapeutic targets in their own right. In order to understand posttranscriptional control of gene expression, RIP-Chip technologies that allow the isolation and identification of mRNAs, microRNAs and protein components of RNP complexes from cell extracts using antibodies to RBPs and microarrays have been developed.
  • Components:
    • Lysis buffer
    • Wash buffer
    • Normal Rabbit IgG
    • High-Salt Solution
    • Solution I
    • Solution II
    • Solution III
    • Solution IV 
  • Description:

    RIP-Assay Kit is optimized for performing the RIP-Chip process.

  • Product Type:
    Kit
  • Short Description:

    RIP-Assay Kit.

  • Size:
    10 Assays
  • Storage Temperature:
    4°C
  • Target:
    RNP Complex
Citations
  1. Zhang C et al. Hepsin inhibits CDK11p58 IRES activity by suppressing unr expression and eIF-2α phosphorylation in prostate cancer. Cell Signal. (2014) In press.,
  2. Banadakoppa M et al. Role of transcription factor Sp1 and RNA binding protein HuR in the downregulation of Dr(+) Escherichia coli receptor protein decay accelerating factor (DAF or CD55) by nitric oxide. FEBS J. 280, 840-54 (2013),
  3. Ferrarese R et al. Lineage-specific splicing of a brain-enriched alternative exon promotes glioblastoma progression. J Clin Invest. 124, 2861-76 (2014),
  4. Hayman TJ et al. Translation initiation factor eIF4E is a target for tumor cell radiosensitization. Cancer Res. 72, 2362-72 (2012),
  5. Janiszewska M et al. Imp2 controls oxidative phosphorylation and is crucial for preserving glioblastoma cancer stem cells. Genes Dev. 26, 1926-44 (2012),
  6. Jin D et al. RNA-binding motif protein 24 regulates myogenin expression and promotes myogenic differentiation. Genes Cells 15, 1158-67 (2010),
  7. Lachke SA et al. Mutations in the RNA granule component TDRD7 cause cataract and glaucoma. Science 331, 1571-6 (2011),
  8. Matsui T et al. Celf1 regulation of dmrt2a is required for somite symmetry and left-right patterning during zebrafish development. Development 139, 3553-60 (2012),
  9. Miyazaki Y et al. Viral delivery of miR-196a ameliorates the SBMA phenotype via the silencing of CELF2. Nat Med. 18, 1136-41 (2012),
  10. Mizutani T et al. 7SK small nuclear ribonucleoprotein complex is recruited to the HIV-1 promoter via short viral transcripts. FEBS Lett. 588, 1630-6 (2014),
  11. Morita M et al. The Lipid Mediator Protectin D1 Inhibits Influenza Virus Replication and Improves Severe Influenza. Cell 153, 112-25 (2013),
  12. Nouvade R et al. Activation of p38 MAPK in CD4 T cells controls IL-17 production and autoimmune encephalomyelitis. Blood 118, 3290-3300 (2011),
  13. Ohno S et al. Polypyrimidine tract-binding protein regulates the cell cycle through IRES-dependent translation of CDK11(p58) in mouse embryonic stem cells. Cell Cycle 10, 3706-13 (2011),
  14. Sasaki-Osugi K et al. Nuclear ALG-2 Interacts with CHERP Ca2+-Dependently and Participates in Regulation of Alternative Splicing of Inositol Trisphosphate Receptor Type 1 (IP3R1) Pre-mRNA. J Biol Chem. 288, 33361-75 (2013),
  15. Tahara N et al. Celf1 is required for formation of endoderm-derived organs in zebrafish. Int J Mol Sci. 14, 18009-23 (2013),
  16. Takagi S et al. RNP2 of RNA Recognition Motif 1 Plays a Central Role in the Aberrant Modification of TDP-43. PLoS One 8, e66966 (2013),
  17. Thompson K et al. Acute adaptive responses of central sensorimotor neurons after spinal cord injury. Translational Neuroscience 1, 268-78 (2010),
  18. Xu L et al. A novel function of RNAs arising from the long terminal repeat of human endogenous retrovirus 9 in cell cycle arrest. J Virol. 87, 25-36 (2013),
  19. Yoo JS et al. DHX36 Enhances RIG-I Signaling by Facilitating PKR-Mediated Antiviral Stress Granule Formation. PLoS Pathog. 10, e1004012 (2014),
  20. Zhang LY et al. MicroRNA-144 promotes cell proliferation, migration and invasion in nasopharyngeal carcinoma through repression of PTEN. Carcinogenesis. 34, 454-63 (2013)