3.4.21.46	C25A	has increased activity compared to the native VEGF-DDELTANDELTAC. Efficiently binds to the soluble receptor VEGFR-2/IgGFc. The C25A mutant behaves mainly as a monomeric protein on SDS-PAGE under reducing conditions but as a dimeric protein under non-reducing conditions. It induces VEGFR-2 Tyr-1175 phosphorylation	698902	
3.4.21.46	C25A/P43S	has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells	698902	
3.4.21.46	C25I	is mainly in a presumably covalently bound dimeric form	698902	
3.4.21.46	C25L	has increased activity compared to the native VEGF-DDELTANDELTAC, the C25L mutant is the most active mutant and is mainly in a presumably covalently bound dimeric form, has highest affinity to bind soluble receptor VEGFR-2/IgGFc. It induces VEGFR-2 Tyr-1175 phosphorylation	698902	
3.4.21.46	C25V	is mainly in a presumably covalently bound dimeric form	698902	
3.4.21.46	C44A	does not bind to the soluble receptor VEGFR-2/IgGFc	698902	
3.4.21.46	C53A	does not bind the soluble receptors VEGFR-2/IgGFc and VEGFR-3/IgGFc	698902	
3.4.21.46	C53A	does not bind to the soluble receptor VEGFR-2/IgGFc	698902	
3.4.21.46	G51C	can not induce cell survival, has increased dimer to monomer ratio	698902	
3.4.21.46	H133A	catalytically inactive	718398