VEGF Human, HEK refers to recombinant human vascular endothelial growth factor (VEGF) isoform 165 (VEGF-165) produced in HEK293 cells. This glycosylated protein contains 165 amino acids (27–191) and has a molecular mass of approximately 40 kDa . Key features include:
Expression Host: HEK293 (human embryonic kidney cell line) .
Glycosylation: Post-translational modifications critical for receptor binding and bioactivity .
Purification: Chromatographic techniques yielding >95% purity by SDS-PAGE .
| Feature | Specification | Source |
|---|---|---|
| Amino Acid Sequence | APMAEGGGQN HHEVVKFMDV... (165 residues) | |
| Molecular Mass | 40 kDa (dimer) | |
| Formulation | Lyophilized from 20 mM PB, 150 mM NaCl |
VEGF Human, HEK is widely used in vascular biology research due to its potent angiogenic properties:
| Assay | Result | Source |
|---|---|---|
| HUVEC Proliferation ED₅₀ | 1.5–12 ng/mL | |
| HUVEC Migration | Dose-dependent motility induction | |
| Vascular Permeability | Increased microvascular leakage |
VEGFR2 Activation: Promotes endothelial cell survival, migration, and tubulogenesis .
Co-receptor Interaction: Binds neuropilin-1 (NRP1), enhancing VEGFR2 signaling in certain contexts .
Proper handling ensures bioactivity retention:
| Parameter | Recommendation | Source |
|---|---|---|
| Lyophilized Storage | -18°C desiccated | |
| Reconstituted Storage | 4°C (2–7 days) or -18°C with HSA/BSA | |
| Reconstitution Buffer | Sterile H₂O (≥100 µg/mL) |
| Condition | Role of VEGF-165 | Evidence Source |
|---|---|---|
| Diabetic Retinopathy | Promotes pathological angiogenesis | |
| Cancer | Tumor vasculogenesis | |
| POEMS Syndrome | Elevated plasma levels |
Vascular Endothelial Growth Factor (VEGF) is a potent growth factor that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. This protein is essential for various physiological processes, including wound healing, embryonic development, and the formation of new blood vessels in response to tissue ischemia. VEGF is also implicated in pathological conditions such as cancer, where it promotes tumor growth by enhancing blood supply to the tumor cells.
VEGF is a glycosylated protein that exists in several isoforms due to alternative splicing of its mRNA. The most studied isoform is VEGF165, which consists of 165 amino acids. This isoform is a dimeric glycoprotein, meaning it is composed of two identical subunits linked together. The molecular weight of VEGF165 is approximately 45 kDa when glycosylated .
Human Embryonic Kidney (HEK) 293 cells are commonly used for the recombinant expression of VEGF. These cells are advantageous because they provide authentic human glycosylation patterns, which are crucial for the stability and biological activity of the protein. The recombinant VEGF produced in HEK 293 cells is often referred to as VEGF (Human Recombinant, HEK) .
VEGF primarily acts on endothelial cells, the cells lining the interior surface of blood vessels. It binds to specific receptors on these cells, initiating a cascade of signaling events that lead to:
VEGF is a critical factor in both physiological and pathological angiogenesis. In cancer, VEGF is often overexpressed, leading to the formation of new blood vessels that supply the tumor with nutrients and oxygen, facilitating its growth and metastasis. Anti-VEGF therapies, such as monoclonal antibodies and small molecule inhibitors, have been developed to target this pathway and are used in the treatment of various cancers .
In addition to its role in cancer, VEGF is also involved in other diseases characterized by abnormal blood vessel growth, such as age-related macular degeneration and diabetic retinopathy. Therapeutic strategies targeting VEGF are being explored for these conditions as well .