• Species Reactivity

  Mouse

• Specificity

  Detects mouse VEGF-B    ₁₆₇ in direct ELISAs and Western blots. In direct ELISAs, approximately 20% cross-reactivity with recombinant human (rh) VEGF-B    ₁₆₇, recombinant mouse (rm) VEGF-B    ₁₈₆, and rmVEGF-D is observed but no cross-reactivity with rmVEGF    ₁₆₅ or rhVEGF-C is observed.

• Source

  Monoclonal Rat IgG    _2A Clone # 128313

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  E. coli-derived recombinant mouse VEGF-B    ₁₆₇    
  Pro22-Gly171    
  Accession # P49766-2

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Western Blot

  1 µg/mL

  Recombinant Mouse VEGF-B    ₁₆₇ (Catalog # )

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Preparation and Storage

• Reconstitution

  Reconstitute at 0.5 mg/mL in sterile PBS.

• Shipping

  The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & 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.

• 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: VEGF-B

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 P  lGF(-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-B  ₁₈₆) is 207 amino acids (aa) in length, with a 21 aa signal sequence and a 186 aa mature region. The short form (VEGF-B  ₁₆₇) 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-B  ₁₈₆ is O-glycosylated; VEGF-B  ₁₆₇ is not. VEGF-B  ₁₆₇ binds heparin; VEGF-B  ₁₈₆ does not. Thus, VEGF-B  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 is 93% and 87% aa identical to bovine and human VEGF-B  ₁₈₆, respectively; mouse VEGF-B  ₁₆₇ is 90% and 88% aa identical to bovine and human VEGF-B  ₁₆₇, respectively. The mouse VEGF-B  ₁₆₇ homodimer is 42 kDa in size, while the VEGF-B  ₁₈₆ homodimer is 62 kDa in size. Unlike VEGF  ₁₆₇, VEGF-B  ₁₈₆ 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-B  ₁₆₇ also binds neuropilin-1, but only the 127 aa processed form of VEGF-B  ₁₈₆ binds neuropilin-1 (10). As a dimer, 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).

• References:

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.

• Long Name:

  Vascular Endothelial Growth Factor B

• Entrez Gene IDs:

  7423 (Human); 22339 (Mouse)

• Alternate Names:

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