Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

VEGF Receptor 1 Antibody #2893

Applications Reactivity Sensitivity MW (kDa) Source
W H Endogenous 180 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

VEGF Receptor 1 Antibody detects endogenous levels of VEGFR-1. This antibody does not cross-react with VEGFR-2 and -3 nor does it detect the sVEGFR-1 variant.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr1307 of human VEGFR-1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from PAE cells transfected with either a mock expression vector or human VEGFR-1, using VEGF Receptor 1 Antibody.

Background

The vascular endothelial growth factor (VEGF) receptor (VEGFR-1, Flt-1) is a 180 kDa receptor tyrosine kinase belonging to the VEGFR (Flt) family (1-3). The receptor is comprised of seven extracellular Ig-like domains, a single transmembrane region and cytoplasmic tail containing the active kinase domain (1,2). VEGFR-1 plays an important role in endothelial cell function and normal vascular development, as well as in hematopoietic function (2,3). VEGF-A is a high affinity ligand of VEGFR-1. VEGFR-1 also binds VEGF-B and PLGF (2). Ligand binding results in very little VEGFR-1 kinase activation, and VEGFR-1/VEGF-A binding negatively regulates VEGF function by diverting the growth factor from other functional VEGF receptors (3).

Two forms of the VEGF receptor 1 are found in cells. Both the membrane-bound form described above and a soluble isoform of VEGFR-1 (sVEGFR-1 or sFlt-1) bind the VEGF ligand with high affinity (4). Full-length VEGFR-1 and the truncated, soluble protein are encoded by the same gene and are generated through differential splicing. Both proteins are associated with an array of human disorders and are potential candidates for therapeutic study (5).

  1. Ferrara, N. et al. (2003) Nat Med 9, 669-76.
  2. Clauss, M. (2000) Semin Thromb Hemost 26, 561-9.
  3. Claesson-Welsh, L. (2003) Biochem Soc Trans 31, 20-4.
  4. Kendall, R.L. et al. (1996) Biochem Biophys Res Commun 226, 324-8.
  5. Shibuya, M. (2006) Angiogenesis 9, 225-30; discussion 231.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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