Human VEGFR-2/KDR (D7), soluble
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Cat-Nr. | S01-002 |
Size | 50 µg |
Price | 320 € |
Source | Insect cells |
Formulation | lyophilized |
Purity Confirmation | > 95% by SDS-PAGE |
Length [aa] | 738 |
Molecular Weight | 116.0 kDa |
N Terminal Sequence | ASVGLPSVSL |
Biological Activity | Measured by its ability to inhibit the VEGF165-induced proliferation in human umbilical vein endothelial (HUVE) cells. |
Species Reactivity | Human |
Buffer | 25mM MES, 100mM NaCl; pH 5.5 |
Reconstitution | The 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 Storage | The 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. |
Synonyms | soluble vascular endothelial growth factor receptor-2 ; soluble CD309; soluble VEGF receptor-2; sKDR |
Description | Recombinant 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 Sequence | ASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGA |
Uniprot ID | P35968 |
Protein RefSeq | NP_002244.1 |
mRNA RefSeq | NM_002253.2 |
Figures
Reference
- 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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