IL10RA Proteins, cDNA Clones Research Reagents

IL10RA (Interleukin 10 Receptor Subunit Alpha, also known as CD210; IL10R; CD210a; CDW210A; HIL-10R; IL-10R1), located on 11q23.3, is a Protein Coding gene. The gene produces a 63003 Da protein composed of 578 amino acids. IL10RA mediates the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. The protein has a signal peptide, extracellular domain, transmembrane domain, and cytoplasmic domain. The human protein shares 60% amino acid identity and 73% similarity with its mouse homolog.

IL10RA Protein (4)

    IL10RA cDNA Clone (52)

    NM_001558.2

    克隆载体 cDNA 产品

    In lentiviral vector

    NM_008348.2

    克隆载体 cDNA 产品

    In lentiviral vector

    NM_057193.2

    克隆载体 cDNA 产品

    In lentiviral vector

    XM_001092736.2

    克隆载体 cDNA 产品

    In lentiviral vector

    IL10RA Lysate (4)

      IL10RA 分子背景

      IL10RA (Interleukin 10 Receptor Subunit Alpha, also known as CD210) is a Protein Coding gene. The protein encoded by this gene is a receptor for interleukin 10. Two transcript variants, one protein-coding, and the other, not protein-coding have been found for this gene. CD210 belongs to the type II cytokine receptor family. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. Activation of CD210 leads to tyrosine phosphorylation of JAK1 and TYK2 kinases. CD210 is broadly expressed in the spleen, bone marrow, and other tissues. Diseases associated with IL10RA include Inflammatory Bowel Disease 28, Autosomal Recessive, and Inflammatory Bowel Disease 28.

      IL10RA 参考文献

      • Josephson K, et al. (2001) Purification, crystallization and preliminary X-ray diffraction of a complex between IL-10 and soluble IL-10R1. Acta Crystallogr D Biol Crystallogr. 57(Pt 12): 1908-11.
      • Tan, J C, et al. (1995) Characterization of recombinant extracellular domain of human interleukin-10 receptor. J Biol Chem. 270(21):12906-11.
      • Josephson, K, et al. (2001) Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site. Immunity. 15(1):35-46.

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