Recombinant Human VEGF-111b Protein, CF Summary
Ala27-Arg131, followed by SLTRKD (B isoform, Reference 7)
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.|
|Reconstitution||Reconstitute at 500 μg/mL in 4 mM HCl.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
When Recombinant Human VEGF R2/KDR Fc Chimera (Catalog # 357-KD) is immobilized at 2 µg/mL, Recombinant Human VEGF111b (Catalog # 10036-VE) binds with an ED50 of 12-72 ng/mL.
2 μg/lane of Recombinant Human VEGF 111b was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 12 kDa and 33 kDa, respectively.
Vascular Endothelial Growth Factor (VEGF or VEGF-A), also known as Vascular Permeability Factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult (1-3). It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues and a cystine knot structure (4). Two families of VEGF isoforms are produced through alternative splicing: VEGF xxx (pro-angiogenic) and VEGF xxxb (anti-angiogenic) families that differ by only six amino-acids at the C-terminal end. The B isoform ends with SLTRKD instead of CDKPRR (5). The first verified and widely reported VEGF xxxb family member is VEGF 165b (6). VEGF 111b is a newly discovered member that is induced by UV-B irradiation or by mitomycin C. It doesn't express in normal conditions and has a remarkable resistance to proteolysis (6). Human VEGF 111b shares 87% aa sequence identity with corresponding regions of mouse and rat VEGF. VEGF 111b contains binding domains for VEGF R1 and VEGF R2, however it lacks binding sites for NRP-1 and heparin and cleavage sites for plasmin and matrix metalloproteinases (7, 8). VEGF 111b has been shown to inhibit the proliferation of HUVECs and ovarian cancer cells as well as migration and tube formation of HUVECs (6-7). It has been demonstrated that VEGF 111b functions through VEGF R2 to inhibit the downstream PI3K, Akt, and ERK1/2 signaling pathways (6, 7).
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