ArticleGrowth factors (Chur, Switzerland)2007
The antibody sc-33040-R fails to specifically recognize phosphorylation of ErbB4 on tyrosine1056.
Article in Growth factors (Chur, Switzerland), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- ErbB4 in the brain: Focus on high grade glioma.Frontiers in oncology · 2022Review
- Convergent and divergent cellular responses by ErbB4 isoforms in mammary epithelial cells.Molecular cancer research : MCR · 2014Article
- The Q43L mutant of neuregulin 2β is a pan-ErbB receptor antagonist.The Biochemical journal · 2012Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation state specific antibodies are important reagents for characterizing protein phosphorylation and signaling. However, these antibodies require proper validation to determine that they do not cross-react with the unphosphorylated peptide or with other phosphoproteins. We have previously shown that phosphorylation of tyrosine1056 of ErbB4 is critical for it to inhibit colony formation on plastic by human tumor cell lines. Thus, an antibody directed against this site would be useful for studying ErbB4 signaling and coupling to biological responses. Here, we demonstrate that a commercially available antibody raised against a phosphopeptide corresponding to the carboxyl-terminal domain of the ErbB4 receptor tyrosine kinase fails to exhibit appropriate specificity. Thus, this antibody does not appear to be suitable for studying ErbB4 phosphorylation or signaling.
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