Mouse VEGF‑B186 Antibody
Mouse VEGF‑B186 Antibody Summary
Accession # P49766.2
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 VFR) is a member of the VEGF-PDGF supergene family of growth factor molecules (1‑4). Five mouse members have been identified, including VEGF-A, -B, -C, -D, and PlGF(-2) (1, 5). VEGF family members are disulfide-linked homo- and heterodimeric proteins that are important regulators of vasculogenesis and lymphangiogenesis. Two isoforms of mouse VEGF-B are produced by alternative splicing (6, 7). The long form (VEGF186) is 207 amino acids (aa) in length, with a putative 21 aa signal sequence and a 186 aa (32 kDa) mature region. The short form (VEGF167) is 188 aa in length, with a 21 aa signal sequence and a 167 aa (21 kDa) mature segment. The two isoforms share the same N-terminal 94 aa residue containing the cysteine knot VEGF homology domain (6‑8). VEGF186 is O-glycosylated; VEGF167 is not. VEGF167 binds heparin; VEGF186 does not. Thus, VEGF186 is secreted and freely diffusible in tissues (7). However, the VEGF-B167 isoform is the predominant form in tissue (9). Mouse VEGF-B186 shares 93% and 87% aa identity with bovine and human VEGF‑B186, respectively. Mouse VEGF-B167 also shares 90% and 88% aa identity with bovine and human VEGF-B167, respectively. Unlike VEGF167, VEGF-B186 can undergo proteolytic processing to generate a partially processed 48 kDa heterodimer (16 kDa and 32 kDa) and a fully processed 32 kDa homodimer (two 16 kDa). Processing appears to occur at Arg 127 of the mature protein (10). VEGF-B can heterodimerize with VEGF (7). Both VEGF-B isoforms can bind to VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3 (11). VEGF-B167 also binds neuropilin-1, but only the 127 aa processed form of VEGF-B186 binds neuropilin-1 (10). As a dimer, the full length VEGF-B186 does not interact with neuropilin-1, while any dimer that contains the processed VEGF-B127 subunit will interact with neuropilin-1 (10). The importance of differential neuropilin binding is unclear. VEGF-B deficient mice display an atrial conduction deficit (12). 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 (11).
- Li, X. and U. Eriksson (2001) Int. J. Biochem Cell Biol. 33:421.
- Olofsson, B. et al. (1999) Curr. Opin. Biotechnol. 10:528.
- Clauss, M. (2000) Semin. Thromb. Hemost. 26:561.
- Matsumoto, T. and L. Claesson-Welsh (2001) Sci STKE Dec. 11(112):RE21.
- DiPalma, T. et al. (1996) Mamm. Genome 7:6.
- Olofsson, B. et al. (1996) Proc. Natl. Acad. Sci. USA 93:2576.
- Olofsson, B. et al. (1996) J. Biol. Chem. 271:19310.
- Twonson, S. et al. (1996) Biochem. Biophys. Res. Commun. 220:922.
- Li, X. et al. (2001) Growth Factors 19:49.
- Makinen, T. et al. (1999) J. Biol. Chem. 274:21217.
- Olofsson, B. et al. (1998) Proc. Nat. Acad. Sci. USA 95:11709.
- Aase, K. et al. (2001) Circulation 104:358.
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