Recombinant Mouse VEGF-B 186 Protein, CF

• Reactivity: Mu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Mouse VEGF-B 186 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized rmFlt-1/Fc Chimera at 1 µg/mL (100 µL/well) can bind rmVEGF-B 186 with a linear range of 0.1-10 ng/mL.
• Source: Spodoptera frugiperda, Sf 21 (stably transfected)-derived mouse VEGF-B protein Gln20-Ala207 & Gln20-Arg148
• Accession #: P49766
• N-terminal Sequence: Gln20
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: VEGFB
• Purity: >90%, 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:
  • Binding Activity
• Theoretical MW: 15.2 kDa.
  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: 28 kDa and 17 kDa, 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 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse VEGF-B 186 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 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. Two isoforms of mouse VEGF-B are produced by alternative splicing (6, 7). The long form (VEGF 186 ) is 207 amino acids (aa) in length, with a putative 21 aa signal sequence and a 186 aa (32 kDa) mature region. The short form (VEGF 167 ) is 188 aa in length, with a 21 aa signal sequence and a 167 aa (21 kDa) mature segment. The two isoforms share the same N-terminal 94 aa residue containing the cysteine knot VEGF homology domain (6 - 8). VEGF 186 is O-glycosylated; VEGF 167 is not. VEGF 167 binds heparin; VEGF 186 does not. Thus, VEGF 186 is secreted and freely diffusible in tissues (7). However, the VEGF-B 167 isoform is the predominant form in tissue (9). Mouse VEGF-B 186 shares 93% and 87% aa identity with bovine and human VEGF-B 186 respectively. Mouse VEGF-B 167 also shares 90% and 88% aa identity with bovine and human VEGF-B 167 respectively. Unlike VEGF 167 VEGF-B 186 can undergo proteolytic processing to generate a partially processed 48 kDa heterodimer (16 kDa and 32 kDa) and a fully processed 32 kDa homodimer (two 16 kDa). Processing appears to occur at Arg 127 of the mature protein (10). VEGF-B can heterodimerize with VEGF (7). Both VEGF-B isoforms can bind to VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3 (11). VEGF-B 167 also binds neuropilin-1, but only the 127 aa processed form of VEGF-B 186 binds neuropilin-1 (10). As a dimer, the full length VEGF-B 186 does not interact with neuropilin-1, while any dimer that contains the processed VEGF-B 127 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).

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. Clauss, M. (2000) Semin. Thromb. Hemost. 26:561. 
4. Matsumoto, T. and L. Claesson-Welsh (2001) Sci .STKE Dec 11 (112):RE21. 
5. DiPalma, T. et al. (1996) Mamm. Genome 7:6. 
6. Olofsson, B. et al. (1996) Proc. Natl. Acad. Sci. USA 93:2576.
7. Olofsson, B. et al. (1996) J. Biol. Chem. 271:19310.
8. Twonson, S. et al. (1996) Biochem. Biophys. Res. Commun. 220:922.
9. Li, X. et al. (2001) Growth Factors 19:49.
10. Makinen, T. et al. (1999) J. Biol. Chem. 274:21217.
11. Olofsson, B. et al. (1998) Proc. Nat. Acad. Sci. USA 95:11709.
12. Aase, K. et al. (2001) Circulation 104:358.

Publications for VEGF-B (767-VE/CF)(5)

Publications using 767-VE/CF

• K Ma, G Singh, J Wang, I O-Sullivan, G Votta-Veli, B Bruce, AN Anbazhagan, AJ van Wijnen, HJ Im Targeting Vascular Endothelial Growth Factor Receptors as a Therapeutic Strategy for Osteoarthritis and Associated Pain International journal of biological sciences, 2023-01-01;19(2):675-690. 2023-01-01 [PMID: 36632459] (Bioassay, Mouse)
• CVJ Box, AK Sandhu, AH Turaihi, P Xiaoké, G Dallinga-T, J Aman, EC Eringa Effects of imatinib on vascular insulin sensitivity and free fatty acid transport in early weight gain PLoS ONE, 2021-07-02;16(7):e0250442. 2021-07-02 [PMID: 34214082] (Bioassay, Human)
• Jang C. A metabolite of branched chain amino acids drives vascular fatty acid transport and causes glucose intolerance. Thesis. 2016-01-01 [PMID: 26950361] (Bioassay, Mouse)
• Poesen K, Lambrechts D, Van Damme P, Dhondt J, Bender F, Frank N, Bogaert E, Claes B, Heylen L, Verheyen A, Raes K, Tjwa M, Eriksson U, Shibuya M, Nuydens R, Van Den Bosch L, Meert T, D'Hooge R, Sendtner M, Robberecht W, Carmeliet P Novel role for vascular endothelial growth factor (VEGF) receptor-1 and its ligand VEGF-B in motor neuron degeneration. J. Neurosci., 2008-10-15;28(42):10451-9. 2008-10-15 [PMID: 18923022] (In Vivo, Mouse)
• 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), Mouse)

Bioinformatics

• Gene Symbol: VEGFB
• Uniprot:
  • P49766()