Species: Hu, Mu, Rt
Host: Rabbit Polyclonal
Analysis of individual DKK domains and chimeric DKKs shows that the carboxy-terminal domains of both DKK1 and DKK2 associate with LRP6 and are necessary and sufficient for Wnt8 inhibition. Xenopus Dickkopf 1 (DKK1) was initially discovered as a Wnt antagonist that plays an important role in head formation. By far, four members of DKK have been identified in mammals. Each DKK molecule contains two conserved cysteine-rich domains. Recent studies showed that the second Cys-rich domains of DKK1 and DKK2 inhibited Wnt3a-activated signaling, whereas the first Cys-rich domains had no effects. In addition, the second Cys-rich domain of DKK2, but not that of DKK1, was able to activate the canonical pathway in the presence of LRP6, and this LRP-dependent signaling does not require Dvl.
|Product By Gene ID
- dickkopf 2
- dickkopf-related protein 2
- dickkopf (Xenopus laevis) homolog 2
- dickkopf related protein-2
- dickkopf homolog 2 (Xenopus laevis)
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