Detects human and mouse VEGF-B in direct ELISAs and Western blots. Recognizes both the VEGF-B167 and VEGF-B186 isoforms. In Western blots, no cross-reactivity with recombinant human (rh) VEGF, rhVEGF-C, rhVEGF-D, rhCTGF, rhPlGF, rhLDGF, or rhPDGF is observed.
Monoclonal Mouse IgG1 Clone # 58013
Protein A or G purified from hybridoma culture supernatant
E. coli-derived recombinant human VEGF-B167 Pro22-Arg188 Accession # AAB06274
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
VEGF‑B167/186 in Human Breast Cancer Tissue. VEGF‑B167/186 was detected in immersion fixed paraffin-embedded sections of human breast cancer tissue using Mouse Anti-Human/Mouse VEGF‑B167/186 Monoclonal Antibody (Catalog # MAB751) at 3 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and cell membranes of cancer cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
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) 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.
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