Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Details of Functionality | Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87:1323. The ED50 for this effect is 7-35 ng/mL. |
Source | Human embryonic kidney cell, HEK293-derived mouse VEGF protein Ala27-Arg214 |
Accession # | |
N-terminal Sequence | Ala27 |
Structure / Form | Disulfide-linked homodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Vegfa |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 22.1 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 28-30 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin. |
Vascular endothelial growth factor (VEGF or VEGF‑A), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult (1‑3). It is a member of the PDGF family that is characterized by a cystine knot structure formed by eight conserved cysteine residues (4). Alternate splicing produces isoforms including 121, 145, 165, 183, 189, and 206 amino acid (aa) forms in humans, with 120, 164 and 188 aa isoforms found in mouse (1‑4). Mouse VEGF188 shares 98% aa sequence identity with the appropriate isoform in rat, and 89% with human, bovine and canine VEGF. While isoforms VEGF120 and VEGF121 are freely diffusible, VEGF188, VEGF189 and VEGF206 contain the highest number of basic aa, which bind heparin and tether these isoforms to the cell surface and extracellular matrix (3‑5). Expression of VEGF188/189 is particularly high in the embryonic lung, where it is produced by type II alveolar epithelia (6). It is thought to be involved in lung, heart and liver vasculogenesis (5, 6). It is not sufficient for vasculogenesis during bone development, but may play a role in bone repair (5, 7). Tumor cell production of VEGF188/189 correlates with poor prognosis (5). VEGF binds the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt‑1) and VEGF R2 (Flk‑1/KDR) on endothelial cells (4). Although affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 4). VEGF188 binds VEGF R2 best when it is cleaved by uPA or plasmin into a 110‑111 aa form (4, 5). Human VEGF165 and VEGF189 also bind the semaphorin receptor Neuropilin‑1 (8, 9).
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