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 0.8-4 ng/mL. |
Source | Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse VEGF protein Ala27-Arg190 |
Accession # | |
N-terminal Sequence | Ala27 |
Structure / Form | Disulfide-linked homodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Vegfa |
Purity | >97%, 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 | 19.4 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 | 42 kDa, non-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 PBS with BSA as a carrier protein. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 50 μg/mL in sterile PBS 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). Alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) have been identified in humans, with 120, 164 and 188 aa isoforms found in mouse (2, 4). Isoforms other than VEGF120 and VEGF121 contain basic heparin-binding regions and are not freely diffusible (4). Mouse VEGF164 shares 97% aa sequence identity with corresponding regions of rat, 89% with human and porcine, 88% with bovine, and 90% with feline, equine and canine VEGF, respectively. 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). Human VEGF165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation with VEGF R2 (5). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4). In adults, VEGF functions mainly in wound healing and the female reproductive cycle (3). Pathologically, it is involved in tumor angiogenesis and vascular leakage (6, 7). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (8). VEGF is induced by hypoxia and cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-alpha (3, 4, 9).
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The application of CD31/Pecam-1 (MEC 7.46) in breast cancer research CD31/PECAM-1, or platelet endothelial cell adhesion molecule 1, is a 130-kDa glycoprotein expressed on vascular and hematopoietic cells. Depending on the cell type, CD31/PECAM-1 expression can be largely localized to cell junctions, playing a rol... Read full blog post. |
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