Human VEGFR-1/Flt-1 (native), soluble

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Size20 µg
Price220 €
SourceInsect cells
Purity Confirmation> 95% by SDS-PAGE
Length [aa]661
Molecular Weight96.0 kDa
N Terminal SequenceSKLKD
Biological ActivityThe activity of sVEGFR-1 was determined by its ability to inhibit the VEGF-A-induced proliferation of HUVECs.
Species ReactivityHuman
ReconstitutionThe lyophilized sVEGFR-1 is soluble in water and most aqueous buffers. The lyophilized sVEGFR-1 should be reconstituted in PBS to a concentration not lower than 100µg/ml.
Stability and StorageLyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sVEGFR-1 should be stored in working aliquots at -70°C. Avoid repeated freeze-thaw cycles!
Synonymssoluble vascular endothelial growth factor receptor-1; soluble FLT1; soluble VEGFR-1
DescriptionRecombinant 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 recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) 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), and 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 split 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 occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC 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.
Uniprot IDP17948
Protein RefSeqNP_001153392
mRNA RefSeqNM_001159920



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  5. Elevated placental soluble vascular endothelial growth factor receptor-1 inhibits angiogenesis in preeclampsia. Shakil Ahmad and Asif Ahmed, Circ Res. 2004 Oct 29;95(9):884-91.

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