Recombinant Human VEGF145 protein

Vascular endothelial growth factor 145 (VEGF145) is a less-studied isoform of the VEGF-A family, a critical regulator of angiogenesis. Generated through alternative splicing of the VEGF-A gene, VEGF145 contains 145 amino acids, distinct from common isoforms like VEGF121 or VEGF165. Its unique structure retains exon 8-encoded sequences, conferring intermediate heparin-binding properties between VEGF121 (non-binding) and VEGF165 (strong binding). This feature enables selective interaction with extracellular matrix components and cell surface receptors.

First identified in the late 1990s, VEGF145 exhibits dual receptor specificity, binding both VEGFR-2 (primary angiogenic signal transducer) and neuropilin-1. Its expression has been detected in placental tissue, certain tumors, and ischemic conditions, suggesting roles in physiological and pathological angiogenesis. Unlike VEGF165. VEGF145 lacks the exon 7-encoded domain, potentially altering its bioavailability and signaling duration.

Recombinant VEGF145 is typically produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications. Researchers utilize it to investigate isoform-specific biological activities, particularly its ability to stimulate endothelial cell proliferation and migration while showing reduced inflammatory effects compared to other VEGF isoforms. Current studies explore its therapeutic potential in cardiovascular regeneration and wound healing, though its precise physiological significance remains less characterized than mainstream VEGF variants. The isoform's balanced matrix-binding properties make it an interesting candidate for localized delivery strategies in tissue engineering applications.