Human VEGFR-1/Flt-1 (D3), soluble
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| Cat-Nr. | S01-015 |
| Size | 5 µg |
| Price | 150 € |
| Source | Insect cells |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 327 |
| Molecular Weight | 45.0 kDa |
| N Terminal Sequence | SKLKD |
| Biological Activity | The activity of sVEGFR-1(D3) was determined by its ability to inhibit the VEGF-A-induced proliferation of HUVECs. |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The lyophilized sVEGFR-1(D3) is soluble in water and most aqueous buffers and should be reconstituted in PBS to a concentration not lower than 100µg/ml. |
| Stability and Storage | Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sVEGFR-1(D3) should be stored in working aliquots at -70°C. |
| Synonyms | soluble vascular endothelial growth factor receptor-1; soluble FLT1; soluble VEGFR-1 |
| Description | Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. 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. |
| Protein Sequence | SKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSY |
| Uniprot ID | P17948 |
| Protein RefSeq | NP_001153392 |
| mRNA RefSeq | NM_001159920 |
Figures
SDS-PAGE analysis of recombinant human soluble VEGFR-1 (D1-3) produced in insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.
Inhibition of the VEGF165-induced proliferation of HUVECs by recombinant human endogenous sFlt-1 and sFlt-1 constructs. HUVECs were stimulated with 10 ng/ml VEGF165, the soluble receptors were added with a 100X excess.
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