The antibody sc-33040-R fails to specifically recognize phosphorylation of ErbB4 on tyrosine1056.
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.
Gallo
Richard M
RM
Purdue School of Pharmacy & Purdue Cancer Research Center, Purdue University, West Lafayette, IN, USA.
Riese
David J
DJ
D000818:Animals; D045163:Antibodies, Phospho-Specific / Q000378:metabolism*; D000918:Antibody Specificity; D045744:Cell Line, Tumor; D066246:ErbB Receptors / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D051379:Mice; D010766:Phosphorylation; D011817:Rabbits; D066247:Receptor, ErbB-4; D014443:Tyrosine / Q000276:immunology / Q000378:metabolism
D045163:Antibodies, Phospho-Specific; D014443:Tyrosine; C587689:ERBB4 protein, human; D066246:ErbB Receptors; C587690:Erbb4 protein, mouse; D066247:Receptor, ErbB-4