Vascular endothelial growth factor receptor 2 Recombinant Protein | KDR recombinant protein

Recombinant Human Vascular endothelial growth factor receptor 2

Cat. Num. AAA967496

• Gene Names: KDR; FLK1; CD309; VEGFR; VEGFR2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Vascular endothelial growth factor receptor 2; Recombinant Human Vascular endothelial growth factor receptor 2; Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; KDR; Protein-tyrosine kinase receptor flk-1; CD309; KDR recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 20-764aa; Extracellular Domain
• Sequence: ASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLE
• Sequence Length: 1356

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for KDR recombinant protein

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hatopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC

Product Categories/Family for KDR recombinant protein

Cancer

References

Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.Arthritis Res. Ther. 10:R73-R73(2008) Alternatively spliced vascular endothelial growth factor receptor-2 is an essential endogenous inhibitor of lymphatic vessel growth.Albuquerque R.J., Hayashi T., Cho W.G., Kleinman M.E., Dridi S., Takeda A., Baffi J.Z., Yamada K., Kaneko H., Green M.G., Chappell J., Wilting J., Weich H.A., Yamagami S., Amano S., Mizuki N., Alexander J.S., Peterson M.L., Brekken R.A., Hirashima M., Capoor S., Usui T., Ambati B.K., Ambati J.Nat. Med. 15:1023-1030(2009) Full length human KDR/flk-1 sequence.Yin L.Y., Wu Y., Patterson C.Coding region for human VEGF receptor KDR (VEGFR-2) .Yu Y., Whitney R.G., Sato J.D. Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Identification of a new endothelial cell growth factor receptor tyrosine kinase.Terman B.I., Carrion M.E., Kovacs E., Rasmussen B.A., Eddy R.L., Shows T.B.Oncogene 6:1677-1683(1991) Cloning and functional analysis of the promoter for KDR/flk-1, a receptor for vascular endothelial growth factor.Patterson C., Perrella M.A., Hsieh C.-M., Yoshizumi M., Lee M.-E., Harber E.J. 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Chem. 274:6453-6460(1999) Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization.Dougher M., Terman B.I.Oncogene 18:1619-1627(1999) Identification of specific molecular structures of human immunodeficiency virus type 1 Tat relevant for its biological effects on vascular endothelial cells.Mitola S., Soldi R., Zanon I., Barra L., Gutierrez M.I., Berkhout B., Giacca M., Bussolino F.J. Virol. 74:344-353(2000) A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells.Takahashi T., Yamaguchi S., Chida K., Shibuya M.EMBO J. 20:2768-2778(2001) Vascular endothelial growth factor-dependent down-regulation of Flk-1/KDR involves Cbl-mediated ubiquitination. Consequences on nitric oxide production from endothelial cells.Duval M., Bedard-Goulet S., Delisle C., Gratton J.P.J. Biol. Chem. 278:20091-20097(2003) Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3) heterodimerization with VEGFR-2 in primary lymphatic endothelial cells regulates tyrosine phosphorylation sites.Dixelius J., Makinen T., Wirzenius M., Karkkainen M.J., Wernstedt C., Alitalo K., Claesson-Welsh L.J. Biol. Chem. 278:40973-40979(2003) The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration.Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N., Matsumoto T., Claesson-Welsh L., Welsh M.J. Biol. Chem. 279:22267-22275(2004) Phosphorylated KDR is expressed in the neoplastic and stromal elements of human renal tumours and shuttles from cell membrane to nucleus.Fox S.B., Turley H., Cheale M., Blazquez C., Roberts H., James N., Cook N., Harris A., Gatter K.J. Pathol. 202:313-320(2004) Vascular endothelial growth factor (VEGF) -D and VEGF-A differentially regulate KDR-mediated signaling and biological function in vascular endothelial cells.Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.J. Biol. Chem. 279:36148-36157(2004) VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis.Matsumoto T., Bohman S., Dixelius J., Berge T., Dimberg A., Magnusson P., Wang L., Wikner C., Qi J.H., Wernstedt C., Wu J., Bruheim S., Mugishima H., Mukhopadhyay D., Spurkland A., Claesson-Welsh L.EMBO J. 24:2342-2353(2005) Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF.Lamalice L., Houle F., Huot J.J. Biol. 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Invest. 118:3904-3916(2008) Transcriptional profiling reveals a critical role for tyrosine phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial cell morphogenesis.Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A., Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L.FASEB J. 23:1490-1502(2009) New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival.Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.Mol. Cell. Biol. 29:241-253(2009) VEGF-dependent tumor angiogenesis requires inverse and reciprocal regulation of VEGFR1 and VEGFR2.Zhang Z., Neiva K.G., Lingen M.W., Ellis L.M., Nor J.E.Cell Death Differ. 17:499-512(2010) Neuroblastoma progression correlates with downregulation of the lymphangiogenesis inhibitor sVEGFR-2.Becker J., Pavlakovic H., Ludewig F., Wilting F., Weich H.A., Albuquerque R., Ambati J., Wilting J.Clin. Cancer Res. 16:1431-1441(2010) VEGF receptor 2/-3 heterodimers detected in situ by proximity ligation on angiogenic sprouts.Nilsson I., Bahram F., Li X., Gualandi L., Koch S., Jarvius M., Soderberg O., Anisimov A., Kholova I., Pytowski B., Baldwin M., Yla-Herttuala S., Alitalo K., Kreuger J., Claesson-Welsh L.EMBO J. 29:1377-1388(2010) The VEGFR2 receptor tyrosine kinase undergoes constitutive endosome-to-plasma membrane recycling.Jopling H.M., Howell G.J., Gamper N., Ponnambalam S.Biochem. Biophys. Res. Commun. 410:170-176(2011) Blood vessel endothelial VEGFR-2 delays lymphangiogenesis an endogenous trapping mechanism links lymph- and angiogenesis.Nakao S., Zandi S., Hata Y., Kawahara S., Arita R., Schering A., Sun D., Melhorn M.I., Ito Y., Lara-Castillo N., Ishibashi T., Hafezi-Moghadam A.Blood 117:1081-1090(2011) Differential roles of vascular endothelial growth factor receptor-1 and receptor-2 in angiogenesis.Shibuya M.J. Biochem. Mol. Biol. 39:469-478(2006) Vascular endothelial growth factor receptor-2 structure, function, intracellular signalling and therapeutic inhibition.Holmes K., Roberts O.L., Thomas A.M., Cross M.J.Cell. Signal. 19:2003-2012(2007) VEGF receptor protein-tyrosine kinases structure and regulation.Roskoski R. Jr.Biochem. Biophys. Res. Commun. 375:287-291(2008) VEGFs and receptors involved in angiogenesis versus lymphangiogenesis.Lohela M., Bry M., Tammela T., Alitalo K.Curr. Opin. Cell Biol. 21:154-165(2009) Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling.Grunewald F.S., Prota A.E., Giese A., Ballmer-Hofer K.Biochim. Biophys. Acta 1804:567-580(2010) Vascular endothelial growth factor receptor-2 in breast cancer.Guo S., Colbert L.S., Fuller M., Zhang Y., Gonzalez-Perez R.R.Biochim. Biophys. 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Med. 14:1236-1246(2008) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 11321597
• NCBI GeneID: 3791
• NCBI Accession #: NP_002244.1
• NCBI GenBank Nucleotide #: NM_002253.2
• UniProt Accession #: P35968; O60723; Q14178; A2RRS0; B5A925; C5IFA0
• Molecular Weight: 110.3 kDa
• NCBI Official Full Name: vascular endothelial growth factor receptor 2
• NCBI Official Synonym Full Names: kinase insert domain receptor
• NCBI Official Symbol: KDR
• NCBI Official Synonym Symbols: FLK1; CD309; VEGFR; VEGFR2
• NCBI Protein Information: vascular endothelial growth factor receptor 2
• UniProt Protein Name: Vascular endothelial growth factor receptor 2
• Protein Family: Vascular endothelial growth factor receptor
• UniProt Gene Name: KDR
• UniProt Synonym Gene Names: FLK1; VEGFR2; VEGFR-2; FLK-1; KDR
• UniProt Entry Name: VGFR2_HUMAN

NCBI Description

Vascular endothelial growth factor (VEGF) is a major growth factor for endothelial cells. This gene encodes one of the two receptors of the VEGF. This receptor, known as kinase insert domain receptor, is a type III receptor tyrosine kinase. It functions as the main mediator of VEGF-induced endothelial proliferation, survival, migration, tubular morphogenesis and sprouting. The signalling and trafficking of this receptor are regulated by multiple factors, including Rab GTPase, P2Y purine nucleotide receptor, integrin alphaVbeta3, T-cell protein tyrosine phosphatase, etc.. Mutations of this gene are implicated in infantile capillary hemangiomas. [provided by RefSeq, May 2009]

Uniprot Description

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.