676490
VEGFR2D1-7, Human, Recombinant, S. frugiperda
Synonym(s):
Vascular Endothelial Growth Factor Receptor 2 D1-7, Soluble KDR/Flk-1
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About This Item
NACRES:
NA.77
UNSPSC Code:
12352202
assay
≥90% (SDS-PAGE)
form
lyophilized
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
solubility
aqueous buffer: ≥100 μg/mL
water: ≥100 μg/mL
shipped in
wet ice
storage temp.
−70°C
Quality Level
Biochem/physiol Actions
Measured by the ability to inhibit VEGF165-induced proliferation in human umbilical vein endothelial (HUVE) cells
Disclaimer
Toxicity: Standard Handling (A)
General description
Recombinant, human VEGFR-2 consisting of all 7 immunoglobulin-like extracellular domains, but lacking the single transmembrane region and the intracellular split tyrosine kinase domain expressed in S. frugiperda insect cells. Contains all of the domains necessary for high affinity binding to VEGF. VEGFR-2 has a lower affinity for VEGF165 than VEGFR-1. However, VEGFR-2 has a higher signaling activity and is reported to mediate almost all observed endothelial cell responses to VEGF, including the increased microvascular permeability and endothelial cell proliferation. VEGFR-2 requires heparin for binding VEGF165.
Other Notes
Robinson, C.J., and Stringer, S.E. 2001 J. Cell Sci.114, 853.
Roeckl, W., et al. 1998. Exp. Cell Res.241, 161.
Roeckl, W., et al. 1998. Exp. Cell Res.241, 161.
Physical form
Lyophilized from 100 mM NaCl, 25 mM MES, pH 5.5.
Preparation Note
Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 6 months at -70°C. Avoid freeze/thaw cycles of solutions.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Melis Denizci Öncü et al.
Biotechnology and applied biochemistry, 69(5), 2122-2137 (2021-10-26)
Development of monoclonal antibody therapeutics against vascular endothelial growth factor receptor 2 (VEGFR-2) protein, which is the main regulator in angiogenesis, has been a major challenge for years. In the current study, we engineer an inclusion body forming single-chain variable
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