|Application ||WB, IF|
|Calculated MW||148098 Da|
|Other Names||Receptor tyrosine-protein kinase erbB-3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, ERBB3, HER3|
|Target/Specificity||A phospho-specific peptide corresponding to residues surrounding Tyrosine 1289 of human HER3/ErbB3 was used as an immunogen. The antibody only detects HER3/ErbB3 phosphorylated on Tyrosine 1289.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HER3/ErbB3 Antibody Phospho (pY1289) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase (PubMed:20682778). May also be activated by CSPG5 (PubMed:15358134).|
|Cellular Location||Isoform 1: Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Epithelial tissues and brain.|
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Provided below are standard protocols that you may find useful for product applications.
HER3/ErbB3 is a member of the ErbB/EGF receptor protein tyrosine kinase family (1,2). Tyrosine phosphorylation of HER3/ErbB3 depends on its association with other ErbB tyrosine kinases (3). Phosphorylation sites in the carboxy-terminal tail mediate downstream signaling pathways. HER3/ErbB3 is highly expressed in many cancer cells (4), and it may work together with other Erb members in tumorigenesis and proliferation (5). HER/ErbB3 is phosphorylated by EGFR or ErbB2 through dimeric interactions with HER/ErbB3, on Tyrosine 1289, a docking site for phosphatidylinositol 3-kinase (6).
1. Katoh, M., et al. Biochem Biophys Res Commun. 192: 1189
2. Kraus, M.H., et al. Proc Natl Acad Sci U S A. 86: 9193
3. Guy, P.M., et al. Proc. Natl. Acad. Sci. USA 91: 8132
4. Sithanandam, G., et al. Carcinogenesis 24: 1581
5. Alimandi, M., et al. Oncogene 10: 1813
6. Jie Zhang, The American Journal of Pathology 170(1), 2007
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