Human VEGFR-2/KDR (D7), soluble

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Cat-Nr.S01-002
Size50 µg
Price320 €
SourceInsect cells
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Length [aa]738
Molecular Weight116.0 kDa
N Terminal SequenceASVGLPSVSL
Biological ActivityMeasured by its ability to inhibit the VEGF165-induced proliferation in human umbilical vein endothelial (HUVE) cells.
Species ReactivityHuman
Buffer25mM MES, 100mM NaCl; pH 5.5
ReconstitutionThe lyophilized human sKDR is soluble in water and most aqueous buffers, it should be reconstituted in water or PBS to a concentration of not lower than 100µg/ml.
Stability and StorageThe material is stable for greater than six months at -20° C to -70° C. After the first thawing it is recommended to aliquote the material, because repeated freeze-thaw cycles will decrease the activity. Store at 4°C not longer than 2 days. Avoid repeated freeze-thaw cycles.
Synonymssoluble vascular endothelial growth factor receptor-2 ; soluble CD309; soluble VEGF receptor-2; sKDR
DescriptionRecombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 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. 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 signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
Protein SequenceASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGA
Uniprot IDP35968
Protein RefSeqNP_002244.1
mRNA RefSeqNM_002253.2

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Reference

  1. Monomeric gremlin is a novel vascular endothelial growth factor receptor-2 antagonist. E. Grillo et al., Oncotarget. 2016 Jun 7; 7(23): 35353–35368.

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