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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.
![Immunocytochemistry Dkk-2 Antibody (994930) [Unconjugated]](http://images.novusbio.com/fullsize/antibody/Dkk2_MAB6628_Immunocytochemistry__Immunofluorescence_23067.jpg)
![Immunohistochemistry Dkk-2 Antibody (994930) [Unconjugated]](http://images.novusbio.com/fullsize/antibody/Dkk2_MAB6628_Immunohistochemistry_23068.jpg)
![Intracellular Staining by Flow Cytometry Dkk-2 Antibody (994930) [Unconjugated]](http://images.novusbio.com/fullsize/antibody/Dkk2_MAB6628_Flow_Cytometry_22980.jpg)
![Bioactivity Dkk-2 [Unconjugated]](http://images.novusbio.com/fullsize/protein/Dkk2_6628DK_1633.jpg)