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A DNA sequence encoding the human splice isoform VEGF-121 protein sequence (containing the signal peptide sequence, and the mature human VEGF-121 sequence) was expressed in modified human 293 cells.

Vascular endothelial growth factor (VEGF, VEGF-A, VPF) is a covalently linked homodimeric glycoprotein (45-48 kDa) that is a member of the cysteine-knot growth factor superfamily. VEGF-121 is a splice variant isoforms of VEGF-A. VEGF-121 is a freely soluble mitogen that does not bind heparin since it lacks two exons (6 and 7), the presence of which confers heparin binding ability. As a consequence, VEGF121 is able to diffuse more freely because it does not bind to heparan-sulfate proteoglycans, yet it is fully active as an inducer of angiogenesis and as a blood vessel permeabilizing agent. Studies have revealed that VEGF-121 is essential for normal embryonic development and plays a major role in the physiological and pathological events of angiogenesis in adults. VEGF-121 has also been shown to play an important role during endochondral bone formation in hypertrophic cartilage remodelling. Structurally, VEGF-121 exists as disulfide linked homodimer and contains 2 potential N-linked glycosylation sites. For a review on the biology of VEGF please refer to Ferrara N et al., (2003) Nat Med. 9(6): 669-76.