Dimeric Growth Factor Receptors
Native-like Structure. Bioactive Performance. Reliable Results.
Conigen’s recombinant growth factor receptors, including VEGFR2 and FGFR1 mimic native conformations essential for signaling studies, therapeutic development, and cancer research.
Growth factor receptors are typically single-pass transmembrane proteins that bind extracellular ligands to regulate cell proliferation, migration, survival, and differentiation. Many function as homo- or heterodimers, activating intracellular pathways such as MAPK and PI3K/Akt. Dysregulation of dimerization, including ligand-independent activation or mutation-driven constitutive signaling, contributes to disease progression in cancer and developmental disorders.
Conigen’s protein dimers enable analysis of ligand binding, antibody specificity, and dimerization-state modulation for precision medicine applications.
Spotlight: VEGFR2
Bioactive Performance
VEGFR2 is a receptor tyrosine kinase that binds VEGF-A to drive angiogenesis and tumor vascularization. Conigen’s VEGFR2 protein dimer mimics native dimerization and shows strong binding to both VEGF-A and VEGFR2-specific antibodies, supporting receptor-ligand and epitope interaction studies.
Immobilized human VEGF-A 2 μg/mL (100 μL/well) can bind human VEGFR2 dimer protein, His-Avi tag (Cat. No. CSP-25127-03), with half maximal effective concentration (EC50) range of 38.8-155.2 μg/mL (QC tested).
These recombinant proteins offer a platform for studying receptor activation dynamics and discovering modulators of dimerization-dependent signaling in cancer and skeletal disorders