Human VEGF-B186 Antibody
Human VEGF-B186 Antibody Summary
Accession # P49765
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Vascular endothelial growth factor B (VEGF-B), also known as vascular endothelial growth factor-related factor (VRF), is a member of the VEGF family of growth factors that share structural and functional similarity (1, 2). Five mammalian members, including VEGF-A, -B, -C, -D and PlGF, have been identified. VEGF family members are disulfide-linked dimeric proteins that are important regulators of physiological and pathological vasculogenesis, angiogenesis and lymphangiogenesis. VEGF-B is expressed in most tissues, especially in heart, skeletal muscle and pancreas. In many tissues, VEGF-B is co-expressed and can heterodimerize with VEGF (3). By alternative splicing, two isoforms of mature VEGF-B containing 167 or 186 amino acid (aa) residues exist (3, 4). The two VEGF-B isoforms have identical amino-terminal cysteine-knot VEGF homology domains but the carboxyl end of VEGF-B167 differs from that of VEGF-B186 by the presence of a highly basic cysteine-rich heparin binding domain. Whereas VEGF-B186 is a secreted diffusible protein, VEGF-B167 is sequestered into the cell matrix after secretion. Both VEGF-B isoforms bind VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3 (5). On endothelial cells, ligation of VEGF R1 by VEGF-B has been shown to regulate the expression and activity of urokinase type plasminogen activator and plasminogen activator inhibitor 1. VEGF-B167 and a proteolytically processed form of VEGF-B186 (VEGF-B127) also bind neuropilin-1 (NP-1), a type I transmembrane receptor for semaphorins/collapsins, ligands involved in neuron guidance (6). Besides VEGF-B, NP-1 has been shown to bind PLGF-2, VEGF165 and VEGF R1 (6, 7). The many interactions of NP-1 with VEGF ligands and receptor suggests that NP-1 may function as a regulator of angiogenesis (7).
- Li, X. and U. Eriksson (2001) Int. J. Biochem Cell Biol. 33:421.
- Olofsson, B. et al. (1999) Curr. Opin. Biotechnol. 10:528.
- Olofsson, B. et al. (1996) Proc. Nat. Acad. Sci. USA 93:2576.
- Grimmond, S. et al. (1996) Benome Res. 6:124.
- Olofsson, B. et al. (1998) Proc. Nat. Acad. Sci. USA 95:11709.
- Makinen, T. et al. (1999) J. Biol. Chem. 274:21217.
- Fuh, G. et al. (2000) J. Biol. Chem. 275:26690.
Citation for Human VEGF-B186 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1.
Authors: Ponticelli S, Marasco D, Tarallo V, Albuquerque RJ, Mitola S, Takeda A, Stassen JM, Presta M, Ambati J, Ruvo M, De Falco S
J. Biol. Chem., 2008;283(49):34250-9.
Sample Types: Recombinant Protein
Applications: ELISA Development
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