Overview

  • Product nameHuman Y14 full length protein

Description

  • NatureRecombinant
  • SourceE. coli
  • Amino Acid Sequence
    • AccessionQ9Y5S9
    • SpeciesHuman
    • SequenceMADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRRLEHHHH HH
    • Molecular weight21 kDa including tags
    • Amino acids1 to 174
    • TagsHis tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab105606 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    Mass Spectrometry

  • Mass spectrometry
    MALDI-TOF
  • Purity> 90 % by SDS-PAGE.
    ab105606 is purified using conventional chromatography techniques.
  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 10% Glycerol, 0.1M Sodium chloride, 20mM Tris HCl, 1mM DTT, pH 8.0

General info

  • Alternative names
    • Binder of OVCA1 1
    • Binder of OVCA1-1
    • BOV 1
    • BOV 1A
    • BOV 1B
    • BOV 1C
    • BOV-1
    • BOV1
    • BOV1A
    • BOV1B
    • BOV1C
    • HSPC 114
    • HSPC114
    • MDS 014
    • MDS014
    • RBM 8
    • RBM 8A
    • RBM 8B
    • RBM8
    • rbm8a
    • RBM8A_HUMAN
    • RBM8B
    • Ribonucleoprotein RBM 8
    • Ribonucleoprotein RBM 8A
    • Ribonucleoprotein RBM8
    • Ribonucleoprotein RBM8A
    • RNA binding motif protein 8
    • RNA binding motif protein 8A
    • RNA binding motif protein 8B
    • RNA binding protein 8A
    • RNA binding protein Y14
    • RNA-binding motif protein 8A
    • RNA-binding protein 8A
    • RNA-binding protein Y14
    • ZNRP
    • ZRNP 1
    • ZRNP1
    see all
  • FunctionComponent of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The heterodimer MAGOH-RBM8A interacts with PYM that function to enhance the translation of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Remains associated with mRNAs in the cytoplasm until the mRNAs engage the translation machinery. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. Complex with MAGOH is a component of the nonsense mediated decay (NMD) pathway.
  • Tissue specificityUbiquitous.
  • Sequence similaritiesBelongs to the RBM8A family.
    Contains 1 RRM (RNA recognition motif) domain.
  • Cellular localizationNucleus. Nucleus speckle. Cytoplasm. Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
  • Information by UniProt

Human Y14 full length protein images

  • 15% SDS-PAGE showing ab105606 (3 µg) at approximately 20.9 kDa.

References for Human Y14 full length protein (ab105606)

ab105606 has not yet been referenced specifically in any publications.

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