Mouse Anti-Human VEGFR1/FLT1 Clone EWF Biotin mAb

Recombinant Human Soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human uMbilical vein endothelial cells. The mature rh-sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96kDa. The soluble receptor consists of the first 6 extracellular domains containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor.

Recombinant human soluble Flt1 (D5)

Centrifuge vial prior to opening. Add sterile distilled water to the vial to fully solubilize the antibody to a concentration of 0.1-1.0 mg/ml.

The unconjugated antibody will detect native human VEGFR-1/Flt-1 in ELISA experiments and on the surface of different human cell types.