• Product nameAnti-KPNA2 antibody
    See all KPNA2 primary antibodies
  • Description
    Chicken polyclonal to KPNA2
  • Tested applicationsSuitable for: WB, ICC/IFmore details
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    Full length protein, corresponding to amino acids 1-529 of KPNA2

  • Positive control
    • KPNA2 recombinant protein.



Our Abpromise guarantee covers the use of ab37628 in the following tested applications.

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

Application Abreviews Notes
WB 1/2000. Predicted molecular weight: 58 kDa.
ICC/IF Use at an assay dependent concentration. PubMed: 22384089


  • FunctionFunctions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
  • Tissue specificityExpressed ubiquitously.
  • Sequence similaritiesBelongs to the importin alpha family.
    Contains 10 ARM repeats.
    Contains 1 IBB domain.
  • DomainConsists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
    The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins.
    The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding.
  • Cellular localizationCytoplasm. Nucleus.
  • Information by UniProt
  • Database links
  • Alternative names
    • IMA1_HUMAN antibody
    • Importin alpha 1 antibody
    • Importin alpha 2 antibody
    • Importin alpha 2 subunit antibody
    • Importin alpha P1 antibody
    • Importin subunit alpha-1 antibody
    • IPO A1 antibody
    • IPOA 1 antibody
    • IPOA1 antibody
    • Karyopherin alpha 2 antibody
    • Karyopherin alpha 2 RAG cohort 1 antibody
    • Karyopherin alpha 2 subunit antibody
    • Karyopherin subunit alpha-2 antibody
    • KPNA2 antibody
    • KPNA2 protein antibody
    • Pendulin antibody
    • QIP 2 antibody
    • QIP2 antibody
    • RAG cohort 1 antibody
    • RAG cohort protein 1 antibody
    • RCH 1 antibody
    • RCH1 antibody
    • SRP 1 antibody
    • SRP1 alpha antibody
    • SRP1 antibody
    • SRP1-alpha antibody
    • SRP1alpha antibody
    see all

Anti-KPNA2 antibody images

  • Anti-KPNA2 antibody (ab37628) at 1/2000 dilution + E coli-derived fusion protein at 2.5 µg

    Goat anti-IgY-HRP dilution at 1/1000 dilution

    Predicted band size : 58 kDa
    Observed band size : 55 kDa (why is the actual band size different from the predicted?)

References for Anti-KPNA2 antibody (ab37628)

This product has been referenced in:
  • Estrada-Bernal A  et al. Functional complexity of the axonal growth cone: a proteomic analysis. PLoS One 7:e31858 (2012). WB, ICC/IF ; Rat . Read more (PubMed: 22384089) »

See 1 Publication for this product

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