Sf9, Baculovirus cells.
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Greater than 90% as determined by SDS-PAGE.
VEGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 987 amino acids (20-764a.a) and having a molecular mass of 110.5kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). VEGFR2 is fused to a 239 amino acids hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Sf9, Baculovirus cells.
ADPASVGLPS VSLDLPRLSI QKDILTIKAN TTLQITCRGQ RDLDWLWPNN QSGSEQRVEV TECSDGLFCK TLTIPKVIGN DTGAYKCFYR ETDLASVIYV YVQDYRSPFI ASVSDQHGVV YITENKNKTV VIPCLGSISN LNVSLCARYP EKRFVPDGNR ISWDSKKGFT IPSYMISYAG MVFCEAKIND ESYQSIMYIV VVVGYRIYDV VLSPSHGIEL SVGEKLVLNC TARTELNVGI DFNWEYPSSK HQHKKLVNRD LKTQSGSEMK KFLSTLTIDG VTRSDQGLYT CAASSGLMTK KNSTFVRVHE KPFVAFGSGM ESLVEATVGE RVRIPAKYLG YPPPEIKWYK NGIPLESNHT IKAGHVLTIM EVSERDTGNY TVILTNPISK EKQSHVVSLV VYVPPQIGEK SLISPVDSYQ YGTTQTLTCT VYAIPPPHHI HWYWQLEEEC ANEPSQAVSV TNPYPCEEWR SVEDFQGGNK IEVNKNQFAL IEGKNKTVST LVIQAANVSA LYKCEAVNKV GRGERVISFH VTRGPEITLQ PDMQPTEQES VSLWCTADRS TFENLTWYKL GPQPLPIHVG ELPTPVCKNL DTLWKLNATM FSNSTNDILI MELKNASLQD QGDYVCLAQD RKTKKRHCVV RQLTVLERVA PTITGNLENQ TTSIGESIEV SCTASGNPPP QIMWFKDNET LVEDSGIVLK DGNRNLTIRR VRKEDEGLYT CQACSVLGCA KVEAFFIIEG AQEKTNLELE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
VEGFR-2 is a cell-surface receptor for VEGFA, VEGFC, and VEGFD. It is predominantly expressed in vascular endothelial cells and is an early marker for endothelial cell progenitors . The receptor consists of an extracellular ligand-binding domain, a single transmembrane helix, and an intracellular tyrosine kinase domain .
VEGFR-2 is the primary mediator of VEGF-induced endothelial proliferation, survival, migration, and tubular morphogenesis . It promotes the reorganization of the actin cytoskeleton and plays an essential role in embryonic hematopoiesis . The signaling and trafficking of VEGFR-2 are regulated by multiple factors, including Rab GTPase, P2Y purine nucleotide receptor, integrin alphaVbeta3, and T-cell protein tyrosine phosphatase .
The recombinant form of VEGFR-2, tagged with a His (histidine) tag, is produced using insect cells as the expression system . This recombinant protein is purified and used in various research applications, including kinase assays and studies on VEGF signaling pathways . The His tag facilitates the purification process and allows for easy detection and quantification of the protein.