The Phospho-VEGF Receptor 2 (Tyr1214) antibody is a specialized tool used to detect the activated form of Vascular Endothelial Growth Factor Receptor 2 (VEGFR2), a critical mediator of angiogenesis. VEGFR2. also known as KDR/Flk-1. is a tyrosine kinase receptor expressed primarily on endothelial cells. Upon binding VEGF ligands (e.g., VEGF-A), the receptor undergoes autophosphorylation at specific tyrosine residues, including Tyr1214. which is located in the kinase insert domain. This phosphorylation event triggers downstream signaling cascades (e.g., MAPK/ERK, PI3K/Akt) that drive endothelial cell proliferation, migration, and survival, essential for blood vessel formation.
The Tyr1214 phosphorylation site is associated with receptor internalization and sustained signaling. Antibodies targeting this phospho-epitope enable researchers to study VEGFR2 activation dynamics in physiological processes (e.g., wound healing, development) and pathological conditions like cancer, diabetic retinopathy, or age-related macular degeneration. Such antibodies are widely used in techniques like Western blotting, immunohistochemistry, or immunofluorescence to assess receptor activation status in cell lines, tissue samples, or preclinical models.
Validating phosphorylation at Tyr1214 provides insights into VEGF pathway regulation, drug targeting efficacy (e.g., anti-angiogenic therapies), and disease mechanisms. Specificity is critical, as transient phosphorylation requires careful sample handling (e.g., protease/phosphatase inhibitors). This antibody thus serves as a key reagent in angiogenesis research and therapeutic development.