Human VEGFR-1/Flt-1 (D5), soluble

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Size5 µg
Price95 €
SourceInsect cells
Purity Confirmation> 90% by SDS-PAGE & visualized by silver stain
Length [aa]536
Molecular Weight70.0 kDa
N Terminal SequenceSGSKLKD
Biological ActivityThe activity of sVEGFR-1(D5) was determined by its ability to inhibit the VEGF-A-induced proliferation of HUVECs.
Species ReactivityHuman
ReconstitutionThe lyophilized human sVEGFR-1(D5) is soluble in water and most aqueous buffers. The lyophilized powder should be reconstituted in water 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(D5) should be stored in working aliquots at -70 °C.
Synonymssoluble vascular endothelial growth factor receptor-1; soluble FLT1; soluble VEGFR-1
DescriptionRecombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. 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 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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