Human VEGFR-1/Flt-1 (D5), soluble
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| Cat-Nr. | S01-011 |
| Size | 5 µg |
| Price | 105 € |
| Source | Insect cells |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 536 |
| Molecular Weight | 70.0 kDa |
| N Terminal Sequence | SKLKD |
| Biological Activity | The activity of sVEGFR-1(D5) was determined by its ability to inhibit the VEGF-A-induced proliferation of HUVECs. |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The 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 Storage | Lyophilized 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. |
| Synonyms | soluble vascular endothelial growth factor receptor-1; soluble FLT1; soluble VEGFR-1 |
| Description | Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (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. |
| Protein Sequence | SKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVN |
| Uniprot ID | P17948 |
| Protein RefSeq | NP_001153392 |
| mRNA RefSeq | NM_001159920 |
Figures
SDS-PAGE analysis of recombinant human soluble VEGFR-1 (D1-5) 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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