With a proven track record in the synthesis of phospho-specific peptides, AnaSpec is pleased to be one of the first companies to introduce a full suite of phospho-specific ErbB-2 (Her-2) polyclonal antibodies. These phosphorylated antibodies show no cross reactivity and are specific for phospho-tyrosine at position 877, 1112, 1222 and 1248 (see dot blot below).

The HER-2/neu, also known as c-erbB2, or CD340 proto-oncogene encodes a 185-kDa transmembrane receptor protein. It has partial homology with the epidermal growth factor receptor and shares intrinsic tyrosine kinase activity with that receptor. HER2 plays a role in oncogenesis in breast, ovarian, gastric, and lung carcinoma and endocrine tumors.

HER2 is constitutively activated in the absence of ligand and signaling occurs through phosphorylation of specific tyrosine residues which serve as docking sites for the adaptor molecules SHC and GRB2 with subsequent activation of Ras-ERK and PI-3K pathways. HER2 activation of the extracellular signal-regulated kinase (ERK) pathway is primarily dependent on phosphorylation of Y^1248/1253 of HER2 and mutation of this residue substantially diminishes the transforming potential of HER2. Other important phosphorylation sites of HER-2 include Y⁸⁷⁷ and Y¹¹¹².  AnaSpec offers
several anti-Her-2/neu (c-erbB2) antibodies developed against the phosphorylated tyrosine-containing Her-2/neu sequences, and corresponding antibodies raised to the same sequence but surrounding non-phosphorylated tyrosine.

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REFERENCES:

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Cobleigh, M. et al J. Clin. Oncol. 17, 2639 (1999).
Castilla-Guerra L. et al. Histopathology  31, 144 (1997).
Yonemura, Y. et al. Cancer  67, 2914 (1991).