This is a research-grade, unconjugated non-therapeutic recombinant analog of ramucirumab, a fully human IgG1 antibody directed against the extracellular domain of human VEGFR2 (KDR, UniProt P35968). It is built to reproduce the binding specificity of the originator molecule so researchers can study VEGFR2 blockade in defined experimental systems, while remaining strictly for research use only and not for human or veterinary use. Supplied unconjugated, it is well suited as a positive control or reference reagent in ligand-blocking and receptor-binding assays, as a benchmarking tool against other anti-VEGFR2 binders, and as a starting point for ADC or bispecific development workflows. The material is offered at research and ultra-low endotoxin grades (typically <1 EU/mg, with <0.5 EU/mg options) and in bulk milligram-to-gram quantities, supporting reproducible in-vitro work and larger preclinical study designs where lot consistency and low endotoxin burden matter. It is a target-directed analog and is not the clinical product.
VEGFR2 (KDR/Flk-1; UniProt P35968) is a receptor tyrosine kinase and the principal signaling receptor for vascular endothelial growth factor A (VEGF-A), and it also binds VEGF-C and VEGF-D. It is expressed predominantly on vascular and lymphatic endothelial cells. Ligand engagement drives receptor dimerization, autophosphorylation of intracellular tyrosine residues, and activation of downstream pathways including PLCgamma-PKC-MAPK, PI3K-AKT, and pathways governing endothelial proliferation, migration, survival, and vascular permeability. Through these outputs VEGFR2 is a central driver of physiological and pathological angiogenesis and lymphangiogenesis. Because tumor neovascularization depends heavily on VEGF-A/VEGFR2 signaling, the receptor is a validated oncology and vascular-biology target, and antibodies that block the ligand-binding extracellular domain interrupt this axis at the receptor level.