Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
Xfz8 is involved in the process of normal epithelium formation in the developing pronephric duct and tubules after specific
Human-chimpanzee differences in a FZD8 enhancer (HARE5) alter cell-cycle dynamics in the developing ne (show WNT2 ELISA Kits)ocortex.
Frizzled-8 has an important pro-inflammatory role and suggest that its expression is related to chronic bronchitis.
report the discovery of a human-accelerated regulatory enhancer (HARE5) of FZD8, a receptor of the Wnt (show WNT2 ELISA Kits) pathway implicated in brain development and size
Study concludes that expression of Fzd8 is repressed in multiple cancers and suggest it may have a role as a tumor suppressor.
c-Met upregulated FZD8 through the ERK/c-Fos cascade in HN-CSC. Taken together, our results offer a preclinical proof-of-concept for targeting the c-Met/FZD8 signaling axis as a CSC-directed therapy to improve HNSCC treatment
We demonstrated an activation of Wnt-2 (show WNT2 ELISA Kits) signaling via the Frizzled-8 receptor in non-small cell lung cancer cells
These observations suggest that c-Jun is involved in APF-mediated inhibition for bladder tumor cell growth
APF has been shown to be a nine-residue frizzled-8 protein-related sialoglycopeptide. Subsequent research has gradually clarified the molecular mechanisms underlying the profound antiproliferative effect of APF.
Soluble FZC18 and Wnt3a (show WNT3A ELISA Kits) physically interact in a cell-free system and soluble FZC18 binds the frizzled 1 (show Fzd1 ELISA Kits) and 8 receptors.
analysis of the frizzled8.Wnt3a.LRP6 signaling complex reveals multiple Wnt (show WNT2 ELISA Kits) and Dkk1 (show DKK1 ELISA Kits) binding sites on LRP6 (show LRP6 ELISA Kits)
molecular model of the Wnt protein binding site on the surface of dimeric CRD (show CRX ELISA Kits) domain of the Fzd8 receptor
Increasing amounts of soluble Frizzled8-cysteine-rich-domain protein modulated Wnt3a (show WNT3A ELISA Kits) signaling in a biphasic manner.
Fzd8 and beta-catenin (show CTNNB1 ELISA Kits) negatively regulate osteoclast differentiation independent of osteoblasts.
Study shows Flamingo (Fmi) and Frizzled (Fz) 8, members of noncanonical Wnt signaling, both express in and functionally maintain quiescent long-term hematopoietic stem cells.
study presents the structure of Xenopus Wnt8 (XWnt8 (show WNT8A ELISA Kits)) in complex with the mouse Fz8-cysteine-rich domain to a resolution of 3.25 A
studies suggest a dose-dependent regulation of signaling by Fz5 and Fz8 in optic fissure/disc formation and progenitor expansion
A major role for frizzled 4 (show FZD4 ELISA Kits) and frizzled 8 in controlling ureteric growth in the developing kidney.
Several lines of evidence that the mouse Cristin/R-spondin family proteins function as Fzd8 and LRP6 (show LRP6 ELISA Kits) receptor ligands and induce the canonical Wnt (show WNT2 ELISA Kits)/beta-catenin (show CTNNB1 ELISA Kits) signaling pathway, leading to TCF (show HNF4A ELISA Kits)-dependent gene activation, are presented.
Molecular modeling of the complex between the xWNT8 (show WNT8A ELISA Kits) protein and the CRD (show CRX ELISA Kits) domain of mFZD8
Insulin-like growth-factor-binding protein-4 (show IGFBP4 ELISA Kits) physically interacted with a Wnt receptor, Frizzled 8 (Frz8), and a Wnt (show WNT2 ELISA Kits) co-receptor, low-density lipoprotein receptor-related protein 6 (LRP6 (show LRP6 ELISA Kits)), and inhibited the binding of Wnt3A (show WNT3A ELISA Kits) to Frz8 and LRP6 (show LRP6 ELISA Kits)
This intronless gene is a member of the frizzled gene family. Members of this family encode seven-transmembrane domain proteins that are receptors for the Wingless type MMTV integration site family of signaling proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway. This gene is highly expressed in two human cancer cell lines, indicating that it may play a role in several types of cancer. The crystal structure of the extracellular cysteine-rich domain of a similar mouse protein has been determined.
, frizzled 8
, frizzled homolog 8
, frizzled 8, seven transmembrane spanning receptor
, frizzled 8 protein