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EpoR is a type I cytokine receptor that initiates signal transduction when its ligand binds. The GEMS receptor is based on a mutated form of the EpoR, that is inert to erythropoietin
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<p>The erythropoietin receptor (EpoR) is a type I cytokine receptor. This receptor induces downstream signaling after binding of its ligand erythropoietin (Epo).<sup>1</sup> The EpoR forms the foundation of the Generalized Extraceullar Molecule Sensor (GEMS) receptor that was developed by Schneller et al., 2018.<sup>2</sup> This part encodes for an EpoR construct that has been designed to develop the GEMS receptor. This construct is a truncated form of the EpoR that has been mutated to render it inert to Epo.<sup>2</sup></p><br><br>
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
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<span class='h3bb'><h2>Sequence and Features</h2></span>
 
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<h2>Usage and Biology</h2>
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<p>The erythropoietin receptor (EpoR) is a type I cytokine receptor,<sup>1</sup> that originates from <i>Homo sapiens (Human)</i>.<sup>3</sup> The EpoR is predominantly expressed on the surface of immature erythroid cells.<sup>1</sup> Together with its ligand Epo, it is the primary regulator of mammalian erythropoiesis (the production of red blood cells).<sup>4</sup> Binding of Epo to the EpoR induces proliferation, survival, and differentiation of erythroid progenitors into red blood cells.<sup>1,4</sup><br>
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When EpoR is in its inactive form, the EpoR dimers are locked by transmembrane helix interactions. This conformation prevents downstream signaling.<sup>2</sup> Binding of the hormone Epo induces reorientation and dimerization of two EpoR monomers, which forms an active dimeric receptor structure (Figure 1). Consequently, signal transduction via Janus Kinase 2 (JAK2) is initiated by the intracellular domains of the EpoR.<sup>1,4</sup>
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Revision as of 12:23, 11 October 2022


EpoR (erythropoietin receptor)

The erythropoietin receptor (EpoR) is a type I cytokine receptor. This receptor induces downstream signaling after binding of its ligand erythropoietin (Epo).1 The EpoR forms the foundation of the Generalized Extraceullar Molecule Sensor (GEMS) receptor that was developed by Schneller et al., 2018.2 This part encodes for an EpoR construct that has been designed to develop the GEMS receptor. This construct is a truncated form of the EpoR that has been mutated to render it inert to Epo.2



Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 289
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 658
    Illegal PstI site found at 289
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 172
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 289
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 289
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage and Biology

The erythropoietin receptor (EpoR) is a type I cytokine receptor,1 that originates from Homo sapiens (Human).3 The EpoR is predominantly expressed on the surface of immature erythroid cells.1 Together with its ligand Epo, it is the primary regulator of mammalian erythropoiesis (the production of red blood cells).4 Binding of Epo to the EpoR induces proliferation, survival, and differentiation of erythroid progenitors into red blood cells.1,4
When EpoR is in its inactive form, the EpoR dimers are locked by transmembrane helix interactions. This conformation prevents downstream signaling.2 Binding of the hormone Epo induces reorientation and dimerization of two EpoR monomers, which forms an active dimeric receptor structure (Figure 1). Consequently, signal transduction via Janus Kinase 2 (JAK2) is initiated by the intracellular domains of the EpoR.1,4