Recombinant Human KDR protein

**Background of KDR Recombinant Protein**

KDR (kinase insert domain receptor), also known as vascular endothelial growth factor receptor 2 (VEGFR2), is a transmembrane tyrosine kinase receptor primarily expressed on endothelial cells. It plays a pivotal role in angiogenesis, the process of new blood vessel formation, by binding to ligands such as VEGF-A, VEGF-C, and VEGF-D. Upon ligand activation, KDR undergoes dimerization and autophosphorylation, triggering downstream signaling pathways like RAS/MAPK and PI3K/AKT, which promote endothelial cell proliferation, migration, and survival. Dysregulation of KDR signaling is implicated in pathological conditions, including cancer, retinopathy, and inflammatory diseases, making it a critical therapeutic target.

Recombinant KDR protein is engineered in vitro using expression systems (e.g., mammalian or insect cells) to produce soluble, functional forms of the receptor. These proteins typically retain key domains, such as the extracellular ligand-binding region, enabling studies on VEGF-KDR interactions. Researchers use KDR recombinant proteins to investigate signaling mechanisms, screen for inhibitory drugs, or develop diagnostic tools. For example, in cancer research, blocking KDR-VEGF interactions can suppress tumor angiogenesis, a strategy leveraged in therapies like bevacizumab.

The production of recombinant KDR involves codon optimization, affinity purification (e.g., via Fc tags), and validation through assays like ELISA or surface plasmon resonance to confirm ligand-binding activity. Its applications extend to basic research, drug discovery, and biomanufacturing, offering insights into vascular biology and aiding the development of targeted therapies. Quality control ensures batch-to-batch consistency, critical for experimental reproducibility and clinical translation. Overall, KDR recombinant proteins serve as indispensable tools for unraveling angiogenesis-related pathways and advancing biomedical innovations.