• Species Reactivity

  Human

• Specificity

  Detects human VEGF-D in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant mouse (rm) VEGF‑D, rmVEGF-B, recombinant human (rh) VEGF-B and rhVEGF is observed.

• Source

  Monoclonal Mouse IgG    ₁ Clone # 78923

• Purification

  Protein A or G purified from ascites

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant human VEGF-D    
  Phe93-Ser201    
  Accession # O43915

• 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.

• Endotoxin Level

  <0.10 EU per 1 μg of the antibody by the LAL method.  

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Immunohistochemistry

  8-25 µg/mL

  See below

• 
  

• Neutralization

  Measured by its ability to neutralize VEGF‑D-induced proliferation in HMVEC human microvascular endothelial cells. Achen, M.     et al. (1998) Proc. Natl. Acad. Sci. USA     95:548. The Neutralization Dose (ND    ₅₀) is typically 3‑8 µg/mL in the presence of 1 µg/mL Recombinant Human VEGF‑D.

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

Data Examples

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-D

Vascular endothelial growth factor D (VEGF-D), also known as c-fos-induced growth factor (FIGF), is a secreted glycoprotein of the VEGF/PDGF family. VEGFs regulate angiogenesis and lymphangiogenesis during development and tumor growth, and are characterized by eight conserved cysteine residues that form a cystine knot structure (1-3). VEGF-C and VEGF-D, which share 23% amino acid (aa) sequence identity, are uniquely expressed as preproproteins that contain long N- and C‑terminal propeptide extensions around the VEGF homology domain (VHD) (1, 2). Proteolytic processing of the 354 aa VEGF-D preproprotein creates a secreted proprotein. Further processing by extracellular serine proteases, such as plasmin or furin-like proprotein convertases, forms mature VEGF-D consisting of non‑covalently linked 42 kDa homodimers of the 117 aa VHD (4-6). Mature human VEGF-D shares 94%, 95%, 99%, 97%, and 93% aa identity with mouse, rat, equine, canine, and bovine VEGF-D, respectively (4, 5). It is expressed in adult lung, heart, muscle, and small intestine, and is most abundantly expressed in fetal lungs and skin (1-4). Mouse and human VEGF-D are ligands for VEGF Receptor 3 (VEGF R3, also called Flt-4) that are active across species and show enhanced affinity when processed (7). Processed human VEGF-D is also a ligand for VEGF R2, also called Flk-1 or KDR (7). VEGF R3 is strongly expressed in lymphatic endothelial cells and is essential for regulation of the growth and differentiation of lymphatic endothelium (1, 2). While VEGF-C is the critical ligand for VEGF R3 during embryonic lymphatic development, VEGF-D is most active in neonatal lymphatic maturation and bone growth (8-10). Both promote tumor lymphangiogenesis (11). Consonant with their activity on VEGF receptors, binding of VEGF-C and VEGF-D to neuropilins contributes to VEGF R3 signaling in lymphangiogenesis, while binding to integrin alpha 9 beta 1 mediates endothelial cell adhesion and migration (12, 13).

• References:

1. Roy, H. et al. (2006) FEBS Lett. 580:2879.

2. Otrock, Z.H. et al. (2007) Blood Cells Mol. Dis. 38:258.

3. Yamada, Y. et al. (1997) Genomics 42:483.

4. Stacker, S.A. et al. (1999) J. Biol. Chem. 274:32127.

5. McColl, B.K. et al. (2003) J. Exp. Med. 198:863.

6. McColl, B.K. et al. (2007) FASEB J. 21:1088.

7. Baldwin, M.E. et al. (2001) J. Biol. Chem. 276:19166.

8. Baldwin, M.E. et al. (2005) Mol. Cell. Biol. 25:2441.

9. Karpanen, T. et al. (2006) Am. J. Pathol. 169:708.

10. Orlandini, M. et al. (2006) J. Biol. Chem. 281:17961.

11. Stacker, S.A. et al. (2001) Nature Med. 7:186.

12. Karpanen, T. et al. (2006) FASEB J. 20:1462.

13. Vlahakis, N.E. et al. (2005) J. Biol. Chem. 280:4544.

• Long Name:

  Vascular Endothelial Growth Factor D/cFos-induced Growth Factor

• Entrez Gene IDs:

  2277 (Human); 14205 (Mouse)

• Alternate Names:

  c-fos induced growth factor (vascular endothelial growth factor D); FIGF; vascular endothelial growth factor D; VEGFD; VEGF-D; VEGF-DVEGFDc-Fos-induced growth factor