This product is an unconjugated, non-therapeutic recombinant analog of gancotamab, an antibody directed against human ERBB2 (HER2), supplied strictly for research use. It is not the clinical drug and is not intended for human or veterinary use. The molecule is built around the same ERBB2 target specificity that defines the originator, making it a convenient reference reagent for in-vitro and preclinical work rather than a therapeutic. As a research-grade tool it is useful for assay development and standardisation: HER2-binding and blocking assays, positive/isotype-relative controls, benchmarking of internally generated anti-HER2 clones, ADCC and antibody-drug-conjugate (ADC) development workflows, and receptor-internalisation or flow-cytometry studies on HER2-expressing cell lines. It is offered at research-grade endotoxin levels (typically <1 EU/mg, with ultra-low <0.5 EU/mg options) and in bulk milligram-to-gram quantities to support screening campaigns, formulation studies, and preclinical model work. Being an unconjugated analog, it can serve as a naked-antibody comparator or as a starting scaffold for conjugation chemistry. All characterisation is for laboratory research only.
ERBB2 (HER2/neu, UniProt P04626) is a member of the EGFR/ErbB family of receptor tyrosine kinases. Unlike its relatives, it has no known high-affinity soluble ligand and instead acts as the preferred heterodimerisation partner for ligand-bound ERBB1 (EGFR), ERBB3, and ERBB4. Dimerisation activates the intracellular kinase domain, driving trans-autophosphorylation and downstream RAS-MAPK and PI3K-AKT signalling that promotes proliferation, survival, and migration. ERBB2 is amplified or overexpressed in a subset of breast and gastric cancers, where high receptor density stabilises active dimers and confers a proliferative and pro-survival advantage. Its extracellular region comprises four subdomains; therapeutic and research antibodies typically engage domain II (the dimerisation arm) or domain IV. This clear cell-surface expression and oncogenic role make ERBB2 a well-validated target for antibody binding, blocking, and effector-function studies.