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Description
VEGF-R2/KDR Fc Chimera Protein, HumanProduct Specification Species Human Accession P35968 Amino Acid Sequence Ala20 Glu764, with C terminal Human IgG1 Fc
Product Specification
| Species | Human |
| Accession | P35968 |
| Amino Acid Sequence |
Ala20-Glu764, with C-terminal Human IgG1 Fc ASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIEGRMDPKSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK |
| Expression System | HEK293 |
| Molecular Weight | 120-140kDa (Reducing) |
| Purity | >95% by SDS-PAGE |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | Human Fc Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4 |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
Background
Vascular endothelial cell growth factor (VEGF) and VEGF receptor 2 (VEGF-R2) are closely related to angiogenesis in glioma. A number of phosphorylated sites, such as Y801, Y951, Y1175, and Y1214 in the VEGF-R2 intracellular domains mediate critical signal transductions, including PI3K/AKT, MAPK, and PKC pathways. Main functions of VEGF-R2 include increasing the expression of VEGF and inducing tumor angiogenesis. In addition, VEGF plays a role in promoting vascular endothelial cell division and angiogenesis through VEGF-R2 and is also involved in promoting the aggressive growth of tumors. In the kidney, VEGF is almost exclusively expressed in glomerular and tubular epithelial cells, while the VEGF-R2 is mainly present in glomerular and tubular endothelial cells, as well as in interstitial cells. The present study shows that VEGF-R2 overexpression in advanced thyroid cancer maintains cancer malignancy and cell survival. Thus, selective targeting of VEGFR2/KDR signaling may be a potential strategy for advanced thyroid cancer treatment.
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