Human VEGFR-2/KDR (native), soluble

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Size5 µg
Price150 €
SourceInsect cells
Purity Confirmation> 95% by SDS-PAGE & visualized by silver stain
Length [aa]659
Molecular Weight105.0 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.
Synonymssoluble vascular endothelial growth factor receptor-2 ; soluble CD309; soluble VEGF receptor-2; sKDR
DescriptionThe naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human soluble VEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 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), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors 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.
Uniprot IDP35968
Protein RefSeqNP_002244.1
mRNA RefSeqNM_002253.2

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