Recombinant Human VEGF-B 167 Protein, CF

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..

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human VEGF-B 167 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Rat Neuropilin‑1 Fc Chimera (Catalog # 566-N1) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human VEGF-B 167 (Catalog # 751-VEB) binds with an ED₅₀ of 10-80 ng/mL.
• Source: E. coli-derived human VEGF-B protein
  Pro22-Arg188
• Accession #: AAA91463
• N-terminal Sequence: Pro22
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 19 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 19-22 kDa, under reducing conditions

Packaging, Storage & Formulations

• 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in HCl with Trehalose.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in 4mM HCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human VEGF-B 167 Protein, CF

• vascular endothelial growth factor B
• VEGFB
• VEGF-B
• VEGF-related factor
• VRFVEGFL

Background

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).

1. Li, X. and U. Eriksson (2001) Int. J. Biochem Cell Biol. 33:421.
2. Olofsson, B. et al. (1999) Curr. Opin. Biotechnol. 10:528.
3. Olofsson, B. et al. (1996) Proc. Nat. Acad. Sci. USA 93:2576.
4. Grimmond, S. et al. (1996) Benome Res. 6:124.
5. Olofsson, B. et al. (1998) Proc. Nat. Acad. Sci. USA 95:11709.
6. Makinen, T. et al. (1999) J. Biol. Chem. 274:21217.
7. Fuh, G. et al. (2000) J. Biol. Chem. 275:26690.

Publications for VEGF-B (751-VEB)(10)

Publications using 751-VEB

• Holm, A;Graus, MS;Wylie-Sears, J;Borgelt, L;Heng Tan, JW;Nasim, S;Chung, L;Jain, A;Sun, M;Sun, L;Brouillard, P;Lekwuttikarn, R;Kozakewich, H;Qi, JY;Teng, JC;Mulliken, JB;Vikkula, M;Francois, M;Bischoff, J; An endothelial SOX18-mevalonate pathway axis enables repurposing of statins for infantile hemangioma bioRxiv : the preprint server for biology 2024-02-02 [PMID: 39026886] (Bioassay, Human)
• Moon, SY;Kim, HJ;Kim, JK;Kim, J;Choi, JS;Won, SY;Park, K;Lee, SHS; An examination of the mechanisms driving the therapeutic effects of an AAV expressing a soluble variant of VEGF receptor-1 PloS one 2024-07-11 [PMID: 38990973] (ELISA Capture, Human)
• Jia, J;Zhu, X;Xue, K;Huang, Y;Wu, M;Yang, Y;Liu, W;Zhang, H;He, L;Sun, H; LncRNA DANCR Enhances Angiogenesis to Promote Melanoma Progression Via Sponging miR-5194 Journal of Cancer 2023-05-05 [PMID: 37215458] (Bioassay, Human)
• Wu L, Meoli C, Mangiafico S, Fazakerley D, Cogger V, Mohamad M, Pant H, Kang M, Powter E, Burchfield J, Xirouchaki C, Mikolaizak A, Stockli J, Kolumam G, van Bruggen N, Gamble J, Le Couteur D, Cooney G, Andrikopoulos S, James D Systemic VEGF-A neutralization ameliorates diet-induced metabolic dysfunction. Diabetes, 2014-04-02;63(8):2656-67. 2014-04-02 [PMID: 24696450] (Bioassay, Human)
• Brave SR, Eberlein C, Shibuya M, Wedge SR, Barry ST Placental growth factor neutralising antibodies give limited anti-angiogenic effects in an in vitro organotypic angiogenesis model. Angiogenesis, 2010-10-16;13(4):337-47. 2010-10-16 [PMID: 20953695] (Bioassay, Human)
• Martino MM, Hubbell JA The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J., 2010-07-29;24(12):4711-21. 2010-07-29 [PMID: 20671107] (Surface Plasmon Resonance, Human)
• Nilsson MB, Zage PE, Zeng L, Xu L, Cascone T, Wu HK, Saigal B, Zweidler-McKay PA, Heymach JV Multiple receptor tyrosine kinases regulate HIF-1alpha and HIF-2alpha in normoxia and hypoxia in neuroblastoma: implications for antiangiogenic mechanisms of multikinase inhibitors. Oncogene, 2010-03-08;29(20):2938-49. 2010-03-08 [PMID: 20208561] (Bioassay, Human)
• Ponticelli S, Marasco D, Tarallo V, Albuquerque RJ, Mitola S, Takeda A, Stassen JM, Presta M, Ambati J, Ruvo M, De Falco S Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1. J. Biol. Chem., 2008-10-15;283(49):34250-9. 2008-10-15 [PMID: 18922791] (ELISA (Standard), Human)
• Narazaki M, Tosato G Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A. Blood, 2006-01-19;107(10):3892-901. 2006-01-19 [PMID: 16424390] (ELISA (Standard))
• Silvestre JS, Tamarat R, Ebrahimian TG, Le-Roux A, Clergue M, Emmanuel F, Duriez M, Schwartz B, Branellec D, Levy BI Vascular endothelial growth factor-B promotes in vivo angiogenesis. Circ. Res., 2003-06-12;93(2):114-23. 2003-06-12 [PMID: 12805240] (In Vivo, Mouse)

Bioinformatics

• Uniprot:
  • AAA91463()