• 产品名称
  • 描述
    兔多克隆抗体to SRP1
  • 宿主
  • 特异性
    ab105346 is predicted not to cross-react with other KPNA family members.
  • 经测试应用
    适用于: ICC/IF, WB, ICCmore details
  • 种属反应性
    与反应: Mouse, Rat, Human
  • 免疫原

    A 15 amino acid synthetic peptide from near the N terminus of Human SRP1 (NP_002255).

  • 阳性对照
    • HeLa cell lysate



Our Abpromise guarantee covers the use of ab105346 in the following tested applications.

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

应用 Ab评论 说明
ICC/IF Use a concentration of 20 µg/ml.
WB Use a concentration of 1 - 2 µg/ml. Predicted molecular weight: 60 kDa.
ICC Use a concentration of 2.5 µg/ml.


  • 功能
    Functions 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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.
  • 组织特异性
    Expressed ubiquitously.
  • 序列相似性
    Belongs to the importin alpha family.
    Contains 10 ARM repeats.
    Contains 1 IBB domain.
  • 结构域
    Consists 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.
  • 翻译后修饰
    Polyubiquitinated in the presence of RAG1 (in vitro).
  • 细胞定位
    Cytoplasm. Nucleus.
  • Information by UniProt
  • 数据库链接
  • 别名
    • IMA5_HUMAN antibody
    • Importin alpha 1 subunit antibody
    • Importin alpha 5 antibody
    • Importin alpha S1 antibody
    • Importin subunit alpha-5, N-terminally processed antibody
    • IPO A5 antibody
    • IPOA 5 antibody
    • IPOA5 antibody
    • Karyopherin alpha 1 antibody
    • Karyopherin alpha 1 subunit antibody
    • Karyopherin subunit alpha-1 antibody
    • KPNA 1 antibody
    • KPNA1 antibody
    • mSRP 1 antibody
    • mSRP1 antibody
    • NPI 1 antibody
    • NPI-1 antibody
    • NPI1 antibody
    • Nucleoprotein interactor 1 antibody
    • RAG cohort protein 2 antibody
    • RCH 2 antibody
    • RCH2 antibody
    • Recombination activating gene cohort 2 antibody
    • SRP 1 antibody
    • SRP1 beta antibody
    • SRP1-beta antibody
    see all


  • Immunofluorescence of SRP1 in K562 cells with ab105346 at 20 ?g/mL.
  • Anti-SRP1 antibody (ab105346) at 1 µg/ml + HeLa cell lysate at 15 µg

    Predicted band size: 60 kDa

  • Immunocytochemistry of SRP1 in HeLa cells with ab105346 at 2.5 µg/ml


ab105346 has not yet been referenced specifically in any publications.


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