Human HER2 protein (extracellular domain), biotinylated, recombinant

Description :
HER2 is also known as receptor tyrosine-protein kinase erbB-2 (v-erb-b2 erythroblastic leukemia viral oncogene homolog 2), metastatic lymph node gene 19 protein, proto-oncogene Neu, p185erbB2. It is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases (RTK). Four members of the EGFR family have been identified: EGFR (ERBB1, HER1), HER2 (ERBB2), HER3 (ERBB3) and HER4 (ERBB4). They typically contain an extracellular ligand binding domain (ECD), a transmembrane domain (TM), and an intracellular kinase domain that can interact with a multitude of signaling molecules and exhibit both ligand-dependent and ligand-independent activity. EGFR signaling is initiated by ligand binding to the extracellular ligand binding domain. This initiates receptor homo-/hetero-dimerization and autophosphorylation by the intracellular kinase domain, resulting in receptor activation. Following activation, phosphorylation of cytoplasmic substrates occurs and a signaling cascade is initiated that drives many cellular responses, including changes in gene expression, cytoskeletal rearrangement, anti-apoptosis and increased cell proliferation. HER2 has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGFR family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways. Amplification or overexpression of HER2 has been reported in multiple cancers, including breast and ovarian tumors. HER2 is the target of several anti-cancer therapeutics.