Recombinant Human VEGF-B 167 Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in HCl with Trehalose.|
|Reconstitution||Reconstitute at 250 μg/mL in 4mM HCl.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Rat Neuropilin‑1 Fc Chimera (Catalog # 566-N1) is immobilized at 1 μg/mL (100 μL/well) Recombinant VEGF-B 167 (Catalog # 751-VEB) binds with an ED50 of 10-80 ng/mL.
1 μg/lane of Recombinant Human VEGF-B 167 (Catalog # 751-VEB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 19-22 kD and 40-45 kDa, respectively..
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.
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