MX2/MXB Antibody Blocking Peptide(bs-10985P)-500ug

MX2/MXB Antibody Blocking Pept

ide(bs-10985P)-500ug
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  • ¥880
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  • bs-10985P
  • 2025年10月16日
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      500ug

    产品编号bs-10985P
    英文名称MX2/MXB Antibody Blocking Peptide
    中文名称干扰素诱导GTP结合蛋白MX2封闭多肽
    英文别名Interferon induced GTP binding protein Mx2; Interferon regulated resistance GTP binding protein MXB; Interferon-induced GTP-binding protein Mx2; Interferon-regulated resistance GTP-binding protein MxB; MX 2; MX dynamin like GTPase 2; Mx2; MX2_HUMAN; MXB; Myxovirus (influenza virus) resistance 2; Myxovirus resistance 2; Myxovirus resistance protein 2; p78 related protein; p78-related protein; Second interferon induced protein p78.
    纯化方法HPLC
    研究领域

    Immunology > Innate Immunity > Cytokines > Interferons

    亚基Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7.
    亚细胞定位Cytoplasm.
    相似性Belongs to the dynamin family.
    Contains 1 GED domain.
    功能May regulate the calcium channel activity of TRPCs. Shows activity against influenza virus and VSV, a rhabdovirus.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    注意事项This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
    背景资料Members of the Dynamin family include GTPase, microtubule-associated proteins that are involved in cellular trafficking, including microtubule bundling and endocytosis. Mx1, also known as MxA, an interferon (IFN)-induced protein, acquires a high degree of resistance to influenza A virus and the rhabdo-virus vesicular stomatitis virus (VSV), which suggests that Mx1 plays an active role against influenza virus and the rhabdovirus VSV. Mx1 is a cytoplasmic protein that is 63% identical to the Mx2 protein, which lacks antiviral activity. Mx2 is also known as MxB and is localized at the cytoplasmic face of nuclear pores. Mx2 expression is not interferon-dependent and this protein is thought to regulate the efficiency and/or kinetics of nuclear import, a function which may have been usurped by its antiviral relatives.

     

     

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