Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble, made in Insect cells

  REL-SFC-006 50 µg

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Human  

Insect cells  

> 90% by SDS-PAGE  

RT  

Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sVEGFR-1/Fc should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles!  

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Description

 

Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. 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. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

 

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