Human VEGFR-1/Flt-1 (D4), soluble

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Cat-Nr.S01-013
Size5 µg
Price130 €
SourceInsect cells
Formulationlyophilized
Purity Confirmation> 90% by SDS-PAGE & visualized by silver stain
Length [aa]457
Molecular Weight55.0 kDa
N Terminal SequenceSGSKLKD
Biological ActivityThe activity of sVEGFR-1(D4) was determined by its ability to inhibit the VEGF-A-induced proliferation of HUVECs.
Species ReactivityHuman
BufferPBS
ReconstitutionThe lyophilized sVEGFR-1(D4) is soluble in water and most aqueous buffers and 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(D4) 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 D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 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 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 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 SequenceSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFC
Uniprot IDP17948
Protein RefSeqNP_001153392
mRNA RefSeqNM_001159920

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