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Recombinant Human Thrombopoietin receptor (MPL), Truncated

The Recombinant Human MPL protein is a protein encoded by recombinant DNA that was cloned in an expression vector that supported the expression of MPL gene. This recombinant MPL protein was expressed in the host. The expression region is 26-491aa of the Human MPL. In the production, the expression vector contains N-terminal 6xHis tag. Every production step was performed with a strict QC system. The purity of this protein is 90%+ determined by SDS-PAGE. The thrombopoietin receptor, MPL, is a member of the type 1 homodimeric cytokine receptor family together with the EPO, prolactin, growth hormone, and granulocyte-colony stimulating factor receptors. Among this receptor family, MPL is unique because it has a reduplicated extracellular CRHD, of which, the distal CRHD is the site of THPO binding. The distal CRHD is also the site of germline SNP causing benign familial thrombocytosis, a hot spot for the mutations causing CAMT as well as the site of terminal sialylation during receptor maturation, which is impaired in the MPN. Like the other hematopoietic growth factor receptors, MPL is responsible for the metabolism of its cognate ligand, but in contrast to the other hematopoietic growth factors, the production of which is mainly regulated by demand. MPL offers a selective therapeutic target in the myeloproliferative neoplasms since impaired MPL processing is unique to the involved stem cells, while MPL is required for hematopoietic stem cell survival and quiescent in their bone marrow niches.

ACP02577

The Recombinant Human MPL protein is a protein encoded by recombinant DNA that was cloned in an expression vector that supported the expression of MPL gene. This recombinant MPL protein was expressed in the host. The expression region is 26-491aa of the Human MPL. In the production, the expression vector contains N-terminal 6xHis tag. Every production step was performed with a strict QC system. The purity of this protein is 90%+ determined by SDS-PAGE. The thrombopoietin receptor, MPL, is a member of the type 1 homodimeric cytokine receptor family together with the EPO, prolactin, growth hormone, and granulocyte-colony stimulating factor receptors. Among this receptor family, MPL is unique because it has a reduplicated extracellular CRHD, of which, the distal CRHD is the site of THPO binding. The distal CRHD is also the site of germline SNP causing benign familial thrombocytosis, a hot spot for the mutations causing CAMT as well as the site of terminal sialylation during receptor maturation, which is impaired in the MPN. Like the other hematopoietic growth factor receptors, MPL is responsible for the metabolism of its cognate ligand, but in contrast to the other hematopoietic growth factors, the production of which is mainly regulated by demand. MPL offers a selective therapeutic target in the myeloproliferative neoplasms since impaired MPL processing is unique to the involved stem cells, while MPL is required for hematopoietic stem cell survival and quiescent in their bone marrow niches.

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Specifications


Cat.No ACP02577 Target NameMPL
Target SynonymsC MPL; CD110; mpl; MPLV; Myeloproliferative leukemia protein; Myeloproliferative leukemia virus oncogene; Proto-oncogene c-Mpl; THCYT2; Thrombopoietin receptor; TPO R; TPO-R; TPOR; TPOR_HUMANFormLiquid or Lyophilized powder
Expression SystemE.coliExpression Range26-491aa
Mol Weight56.5kDaProtein LengthExtracellular Domain
PurityGreater than 90% as determined by SDS-PAGE.Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDP40238
Background Information
  • Uniprot Id

    P40238

  • Target Species

    Human

  • Target Name

    MPL

  • Target Full Name

    Thrombopoietin receptor

  • Target Function

    Receptor for thrombopoietin that acts as a primary regulator of megakaryopoiesis and platelet production. May represent a regulatory molecule specific for TPO-R-dependent immune responses.

  • Target Involvement

    Congenital amegakaryocytic thrombocytopenia (CAMT); Thrombocythemia 2 (THCYT2); Myelofibrosis with myeloid metaplasia (MMM)

  • Target Subcellular Location

    Cell membrane; Single-pass type I membrane protein. Golgi apparatus. Cell surface.

  • Target Protein Families

    Type I cytokine receptor family, Type 1 subfamily

  • Target Tissue Specificity

    Expressed at a low level in a large number of cells of hematopoietic origin. Isoform 1 and isoform 2 are always found to be coexpressed.

  • Target Research Area

    Immunology

  • Target Synonyms

    C MPL; CD110; mpl; MPLV; Myeloproliferative leukemia protein; Myeloproliferative leukemia virus oncogene; Proto-oncogene c-Mpl; THCYT2; Thrombopoietin receptor; TPO R; TPO-R; TPOR; TPOR_HUMAN

  • Target Background

    In 1990 an oncogene, v-mpl, was identified from the murine myeloproliferative leukemia virus that was capable of immortalizing bone marrow hematopoietic cells from different lineages. In 1992 the human homologue, named, c-mpl, was cloned. Sequence data revealed that c-mpl encoded a protein that was homologous with members of the hematopoietic receptor superfamily. Presence of anti-sense oligodeoxynucleotides of c-mpl inhibited megakaryocyte colony formation. The ligand for c-mpl, thrombopoietin, was cloned in 1994. Thrombopoietin was shown to be the major regulator of megakaryocytopoiesis and platelet formation. The protein encoded by the c-mpl gene, CD110, is a 635 amino acid transmembrane domain, with two extracellular cytokine receptor domains and two intracellular cytokine receptor box motifs . TPO-R deficient mice were severely thrombocytopenic, emphasizing the important role of CD110 and thrombopoietin in megakaryocyte and platelet formation. Upon binding of thrombopoietin CD110 is dimerized and the JAK family of non-receptor tyrosine kinases, as well as the STAT family, the MAPK family, the adaptor protein Shc and the receptors themselves become tyrosine phosphorylated.

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