Recombinant Proteins

USD 280.00

2 Weeks

The recombinant Human VEGF-C contains 129 amino acids residues and was fused to a His-tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions.

Tag Tag Free
Expression Host Sf9

USD 180.00

2 Weeks

The recombinant Human VEGF-C contains 129 amino acids residues and was fused to a His-tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions.

Tag Tag Free
Expression Host Sf9

VEGF-C152S is a point mutant generated by the replacement of the second conserved Cys residue of the recombinant processed VEGF-C by a Ser residue. VEGF-C152S is analog to the human VEGF-C156S mutant and only active toward VEGFR-3/FLT-4 but, unlike wild type VEGF-C, is unable to bind to and to activate signalling through VEGFR-2/KDR. VEGF-C152S was inactive in the vascular permeability assay and did not increase migration of the capillary endothelial cells, indicating that these VEGF-like effects of VEGF-C require VEGFR-2 binding.

Tag Tag Free
Expression Host Sf9

USD 310.00

2 Weeks

The recombinant Rat VEGF-C contains 115 amino acids residues and was fused to a His-tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 15-20 kDa protein in SDS-PAGE under reducing conditions.

Tag Tag Free
Expression Host Sf9

USD 200.00

2 Weeks

The recombinant Rat VEGF-C contains 115 amino acids residues and was fused to a His-tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 15-20 kDa protein in SDS-PAGE under reducing conditions.

Tag Tag Free
Expression Host Sf9

VEGF-C152S is a point mutant generated by the replacement of the second conserved Cys residue of the recombinant processed VEGF-C by a Ser residue. VEGF-C152S is analog to the human VEGF-C156S mutant and only active toward VEGFR-3/FLT-4 but, unlike wild type VEGF-C, is unable to bind to and to activate signalling through VEGFR-2/KDR. VEGF-C152S was inactive in the vascular permeability assay and did not increase migration of the capillary endothelial cells, indicating that these VEGF-like effects of VEGF-C require VEGFR-2 binding.

Tag Tag Free
Expression Host Sf9