Recombinant Human VEGF-121

Cat No. Size Price Add Cart
HVG-VF1-0010 10ug $ 205.00 Add Cart
HVG-VF1-0100 100ug $ 1615.00 Add Cart
HVG-VF1-1000 1000ug $ 4225.00 Add Cart

Product Specifications

•      Expression of Human Proteins in Human Cells

•      Extreme low Endotoxin

•      High Purity

•      Animal Free and Xeno Free

•      Tag Free

Source: Human cells derived

Structure: Glycosylated homodimer

Purity: >95% by SDS-PAGE

Endotoxin Level: <0.5EU/ug

Molecular  Weight:  37kDa  homodimer,  50kDa homotrimer

Formulation: Lyophilized from a 0.2μm filtered solution in PBS without carrier protein


Activity Assay

The activity was measured by its ability to stimulate the proliferation of HUVEC cells (Human Umbilical Vein Endothelial Cells).



Briefly centrifuge the vial before opening. It is recommended to reconstitute the protein in sterile PBS containing 0.1% endotoxin-free recombinant human serum albumin.


Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. In general: 12 months from date of receipt, -20 to -80°C as supplied. 1 month, 2 to 8°C under sterile conditions after reconstitution. 3 months, -20 to -80°C under sterile conditions after reconstitution.


Protein Description

Vascular endothelial  growth  factor  (VEGF)  is a potent growth and angiogenic cytokine. It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues and a cystine knot structure VEGF stimulates angiogenesis, vasculogenesis and  endothelial cell growth, induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Human express alternately spliced isoforms, and VEGF-121 is the only form that lacks a basic heparin binding region and is freely diffusible. VEGF-121 induces the proliferation of lymphatic endothelial cells and the lymph angiogenesis may be promoted by up regulation of VEGF-121.



Leung DW, et al. (1989) Science 246:1306-1309.

Robinson CJ, et al. (2001) J. Cell. Sci. 114:853.

Tischer E, et al. (1991) J. Biol. Chem. 266,11947-11954.

Byrne AM, et al. (2005) J. Cell. Mol. Med. 9,777