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 Y1248/1253
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.
Request AnaSpec’s newest
Antibodies Brochure today
Coussens L. et al. Science 230,1132 (1985).
Cobleigh, M. et al J. Clin. Oncol. 17,
Castilla-Guerra L. et al. Histopathology 31,
Yonemura, Y. et al. Cancer 67, 2914 (1991).