United Kingdom (UK)
Recombinant monoclonal antibody to Frizzled. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma 1C11-B9-H9-G9-D9.
UniProt Accession Number of Target Protein: P18537
Alternative Name(s) of Target: Frizzled protein; fz; Frizzled-1; dFz1
Immunogen: The mouse version of this antibody was generated by immunizing a mouse with amino acids 1-252 of Drosophila Frizzled.
Specificity: This antibody is specific for drosophila frizzled. It is specific for amino acids 1-252. Frizzled is a receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes.
Application Notes: To study the biochemical characteristics of the frizzled protein. Proteins from schneider 2 cells were immunoprecipitated using the mouse version of this antibody. Futhermore the precipitates were immunoblotted using this antibody. Finally both schneider cells and pupal wings were immunostained using this antibody (Park et al, 1994; pmid:8199049). Protein lysates from drosophila L cells were immunoblotted using the mouse version of this antibody (Pradhan-Sundd and Verheyen, 2015; pmid:26224310). Adult drosophila wings were immunostained using the mouse version of this antibody (Adler et al, 1997; pmid:9382848). To determine the link between the wingless and the frizzled proteins. A immunolabeling was preformed on drosophila embryos using this antibody (Müller et al, 1999; pmid:9876186). To understand the wingless pathway. P19 cell lysates were immunoblotted using this antibody (Abdul-Ghani et al, 2011; pmid:21041481).
Antibody first published in:
Park et al. The frizzled gene of Drosophila encodes a membrane protein with an odd number of transmembrane domains Mech Dev. 1994 Feb;45(2):127-37. PMID:8199049
Note on publication:
To study the biochemical characteristics of this rare protein, we constructed a hs-fz fusion gene and transferred this to Drosophila tissue culture cells and embryos. Cell fractionation experiments and immunostaining experiments showed that the Fz protein is an integral membrane protein containing an odd number of transmembrane domains, consistent with previous suggestions that it contains seven transmembrane domains.