Recombinant Mouse VEGF-B 167 Protein


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Recombinant Mouse VEGF-B 167 Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rrNeuropilin-1/Fc Chimera at 4 µg/mL (100 µL/well) can bind rmVEGF-B167 with a linear range of 0.8‑50 ng/mL.
E. coli-derived mouse VEGF-B protein
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


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.
Read Publications using
2595-VE in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Mouse VEGF-B 167 Protein

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


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. Mouse VEGF-B has two isoforms, a 32 kDa single chain and a 21 kDa single chain form (6, 7). The long form (VEGF-B186) is 207 amino acids (aa) in length, with a 21 aa signal sequence and a 186 aa mature region. The short form (VEGF-B167) is 188 aa in length, with a 21 aa signal sequence and a 167 aa mature segment. Each mature isoform shows the same N-terminal 94 aa that contains a cysteine knot VEGF homology domain (6 - 8). VEGF-B186 is O-glycosylated; VEGF-B167 is not. VEGF-B167 binds heparin; VEGF-B186 does not. Thus, VEGF-B186 is secreted and freely diffusible in tissues (7). However, the VEGF-B167 isoform is the predominant form in tissue (9). Mouse VEGF-B186 is 93% and 87% aa identical to bovine and human VEGF-B186, respectively; mouse VEGF-B167 is 90% and 88% aa identical to bovine and human VEGF-B167, respectively. The mouse VEGF-B167 homodimer is 42 kDa in size, while the VEGF-B186 homodimer is 62 kDa in size. Unlike VEGF167, VEGF-B186 undergoes proteolytic processing that creates a partially processed 48 kDa homodimer and a fully processed 32 kDa homodimer. Processing appears to occur at Arg127 of the mature form (10). Both forms of VEGF-B can heterodimerize with VEGF (7). Both VEGF-B isoforms bind to VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3 (11). VEGF-B167 also binds neuropilin-1, but only the 127 aa processed form of VEGF-B186 binds neuropilin-1 (10). As a dimer, full length VEGF-B186 does not interact with neuropilin-1, while any dimer that contains the processed VEGF-B127 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.

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Publications for VEGF-B (2595-VE)(2)

We have publications tested in 1 confirmed species: Rat.

We have publications tested in 2 applications: Bioassay, In Vivo.

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Gene Symbol Vegfa