< 1.0 EU per μg of the protein as determined by the LAL method
1. Measured by its binding ability in a functional ELISA. Immobilized recombinant human VEGFA at 1.25 μg/ml (100 μl/well) can bind VEGFR2 with a linear range of 1.25-40.0 ng/ml. 2. Measured by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is typically 20-120 ng/mL in the presence of 10 ng/mL recombinant human VEGF165.
A DNA sequence encoding the extracellular domain of human VEGFR2 (NP_002244.1) (Met 1-Glu 764) was fused with the Fc region of human IgG1 at the C-terminus.
The recombinant human VEGFR2/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 979 amino acids and predicts a molecular mass of 109 kDa. The apparent molecular mass of rh VEGFR2/Fc monomer is approximatly 150-160 in SDS-PAGE under reducing conditions.
Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. 2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
稳定性 & 储存条件
Samples are stable for up to twelve months from date of receipt at -70℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
VEGFR2, also called as KDR or Flk-1, is identified as the receptor for VEGF and VEGFC and an early marker for endothelial cell progenitors, whose expression is restricted to endothelial cells in vivo. VEGFR2 was shown to be the primary signal transducer for angiogenesis and the development of pathological conditions such as cancer and diabetic retinopathy. It has been shown that VEGFR2 is expressed mainly in the endothelial cells, and the expression is upregulated in the tumor vasculature. Thus the inhibition of VEGFR2 activity and its downstream signaling are important targets for the treatment of diseases involving angiogenesis. VEGFR2 transduces the major signals for angiogenesis via its strong tyrosine kinase activity. However, unlike other representative tyrosine kinase receptors, VEGFR2 does not use the Ras pathway as a major downstream signaling but rather uses the phospholipase C-protein kinase C pathway to signal mitogen-activated protein (MAP)-kinase activation and DNA synthesis. VEGFR2 is a direct and major signal transducer for pathological angiogenesis, including cancer and diabetic retinopathy, in cooperation with many other signaling partners; thus, VEGFR2 and its downstream signaling appear to be critical targets for the suppression of these diseases. VEGF and VEGFR2-mediated survival signaling is critical to endothelial cell survival, maintenance of the vasculature and alveolar structure and regeneration of lung tissue. Reduced VEGF and VEGFR2 expression in emphysematous lungs has been linked to increased endothelial cell death and vascular regression.