Human VEGFR-1/Flt-1 (D3)-His, soluble

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Cat-Nr.S01-080
Size50 µg
Price490 €
CategorySoluble Receptors
SourceInsect cells
LabelHis-Tag
Species ReactivityHuman
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE & visualized by Coomassie stain
Length [aa]327
Molecular Weight40.0 kDa
N Terminal SequenceSGSKLKD
BufferPBS
ReconstitutionCentrifuge the vial prior to opening! The lyophilized sVEGFR-1(D3)-His is soluble in water and most aqueous buffers and should be reconstituted in water to a concentration not lower than 100ng/ml.
Stability and StorageLyophilized 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.
Synonymssoluble vascular endothelial growth factor receptor-1; soluble FLT1; soluble VEGFR-1
DescriptionRecombinant 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 HUVE 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 SequenceSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRR
Uniprot IDP17948
Protein RefSeqNP_001153392
mRNA RefSeqNM_001159920

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