Mouse VEGF-B167/186 Alexa Fluor® 594-conjugated Antibody Summary
Pro22-Ala107
Accession # P49766
Applications
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.
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Background: VEGF-B
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. Mouse VEGF-B has two isoforms, a 32 kDa single chain and a 21 kDa single chain form (6, 7). The long form (VEGF-B186) is 207 amino acids (aa) in length, with a 21 aa signal sequence and a 186 aa mature region. The short form (VEGF-B167) is 188 aa in length, with a 21 aa signal sequence and a 167 aa mature segment. Each mature isoform shows the same N-terminal 94 aa that contains a cysteine knot VEGF homology domain (6 - 8). VEGF-B186 is O-glycosylated; VEGF-B167 is not. VEGF-B167 binds heparin; VEGF-B186 does not. Thus, VEGF-B186 is secreted and freely diffusible in tissues (7). However, the VEGF-B167 isoform is the predominant form in tissue (9). Mouse VEGF-B186 is 93% and 87% aa identical to bovine and human VEGF-B186, respectively; mouse VEGF-B167 is 90% and 88% aa identical to bovine and human VEGF-B167, respectively. The mouse VEGF-B167 homodimer is 42 kDa in size, while the VEGF-B186 homodimer is 62 kDa in size. Unlike VEGF167, VEGF-B186 undergoes proteolytic processing that creates a partially processed 48 kDa homodimer and a fully processed 32 kDa homodimer. Processing appears to occur at Arg127 of the mature form (10). Both forms of VEGF-B can heterodimerize with VEGF (7). Both VEGF-B isoforms 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, 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).
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