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Vascular Endothelial Growth Factor Receptor 2 (KDR) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS967496

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,… More details

$230 / 0.02 mg (Mammalian-Cell) +1 FREE 8GB USB
Product Documentation
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Vascular endothelial growth factor receptor 2 (KDR), Recombinant Protein
Full Product Name
Recombinant Human Vascular endothelial growth factor receptor 2
Product Gene Name
Product Synonym Names
Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; KDR; Protein-tyrosine kinase receptor flk-1; CD309
Sequence
ASVGLPSVSL DLPRLSIQKD ILTIKANTTL QITCRGQRDL DWLWPNNQSG SEQRVEVTEC SDGLFCKTLT IPKVIGNDTG AYKCFYRETD LASVIYVYVQ DYRSPFIASV SDQHGVVYIT ENKNKTVVIP CLGSISNLNV SLCARYPEKR FVPDGNRISW DSKKGFTIPS YMISYAGMVF CEAKINDESY QSIMYIVVVV GYRIYDVVLS PSHGIELSVG EKLVLNCTAR TELNVGIDFN WEYPSSKHQH KKLVNRDLKT QSGSEMKKFL STLTIDGVTR SDQGLYTCAA SSGLMTKKNS TFVRVHEKPF VAFGSGMESL VEATVGERVR IPAKYLGYPP PEIKWYKNGI PLESNHTIKA GHVLTIMEVS ERDTGNYTVI LTNPISKEKQ SHVVSLVVYV PPQIGEKSLI SPVDSYQYGT TQTLTCTVYA IPPPHHIHWY WQLEEECANE PSQAVSVTNP YPCEEWRSVE DFQGGNKIEV NKNQFALIEG KNKTVSTLVI QAANVSALYK CEAVNKVGRG ERVISFHVTR GPEITLQPDM QPTEQESVSL WCTADRSTFE NLTWYKLGPQ PLPIHVGELP TPVCKNLDTL WKLNATMFSN STNDILIMEL KNASLQDQGD YVCLAQDRKT KKRHCVVRQL TVLERVAPTI TGNLENQTTS IGESIEVSCT ASGNPPPQIM WFKDNETLVE DSGIVLKDGN RNLTIRRVRK EDEGLYTCQA CSVLGCAKVE AFFIIEGAQE KTNLE
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
110.3 kDa
Sequence Positions
20-764aa; Extracellular Domain
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
191306
3D Structure
ModBase 3D Structure for P35968

Product Categories/Family for KDR recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for KDR recombinant protein

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. Biol. Chem. 270:23111-23118(1995) Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor.Terman B.I., Dougher-Vermazen M., Carrion M.E., Dimitrov D., Armellino D.C., Gospodarowicz D., Boehlen P.Biochem. Biophys. Res. Commun. 187:1579-1586(1992) Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor.Waltenberger J., Claesson-Welsh L., Siegbahn A., Shibuya M., Heldin C.H.J. Biol. Chem. 269:26988-26995(1994) The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the PLC-gamma pathway and partially induces mitotic signals in NIH3T3 fibroblasts.Takahashi T., Shibuya M.Oncogene 14:2079-2089(1997) VEGF-A induces expression of eNOS and iNOS in endothelial cells via VEGF receptor-2 (KDR) .Kroll J., Waltenberger J.Biochem. Biophys. Res. Commun. 252:743-746(1998) Vascular endothelial growth factor regulates endothelial cell survival through the phosphatidylinositol 3'-kinase/Akt signal transduction pathway. Requirement for Flk-1/KDR activation.Gerber H.P., McMurtrey A., Kowalski J., Yan M., Keyt B.A., Dixit V., Ferrara N.J. Biol. Chem. 273:30336-30343(1998) A novel function of VEGF receptor-2 (KDR) rapid release of nitric oxide in response to VEGF-A stimulation in endothelial cells.Kroll J., Waltenberger J.Biochem. Biophys. Res. Commun. 265:636-639(1999) Vascular endothelial growth factor receptor KDR tyrosine kinase activity is increased by autophosphorylation of two activation loop tyrosine residues.Kendall R.L., Rutledge R.Z., Mao X., Tebben A.J., Hungate R.W., Thomas K.A.J. Biol. 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. Chem. 281:34009-34020(2006) Intrinsic tyrosine kinase activity is required for vascular endothelial growth factor receptor 2 ubiquitination, sorting and degradation in endothelial cells.Ewan L.C., Jopling H.M., Jia H., Mittar S., Bagherzadeh A., Howell G.J., Walker J.H., Zachary I.C., Ponnambalam S.Traffic 7:1270-1282(2006) Phosphorylation of tyrosine 801 of vascular endothelial growth factor receptor-2 is necessary for Akt-dependent endothelial nitric-oxide synthase activation and nitric oxide release from endothelial cells.Blanes M.G., Oubaha M., Rautureau Y., Gratton J.P.J. Biol. Chem. 282:10660-10669(2007) AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice.Zhang H., He Y., Dai S., Xu Z., Luo Y., Wan T., Luo D., Jones D., Tang S., Chen H., Sessa W.C., Min W.J. Clin. 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. Acta 1806:108-121(2010) Tyrosine kinase receptor Flt/VEGFR family its characterization related to angiogenesis and cancer.Shibuya M.Genes Cancer 1:1119-1123(2010) Signal transduction by vascular endothelial growth factor receptors.Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.Biochem. J. 437:169-183(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Programmed cell death 6 (PDCD6) inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2.Rho S.B., Song Y.J., Lim M.C., Lee S.H., Kim B.R., Park S.Y.Cell. Signal. 24:131-139(2012) VEGFR2 functions as an H(2) S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells.Tao B.B., Liu S.Y., Zhang C.C., Fu W., Cai W.J., Wang Y., Shen Q., Wang M.J., Chen Y., Zhang L.J., Zhu Y.Z., Zhu Y.C.Antioxid. Redox Signal. 19:448-464(2013) Vascular endothelial cell growth-activated XBP1 splicing in endothelial cells is crucial for angiogenesis.Zeng L., Xiao Q., Chen M., Margariti A., Martin D., Ivetic A., Xu H., Mason J., Wang W., Cockerill G., Mori K., Li J.Y., Chien S., Hu Y., Xu Q.Circulation 127:1712-1722(2013) Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2 a key enzyme in angiogenesis.McTigue M.A., Wickersham J.A., Pinko C., Showalter R.E., Parast C.V., Tempczyk-Russell A., Gehring M.R., Mroczkowski B., Kan C.-C., Villafranca J.E., Appelt K.Structure 7:319-330(1999) Novel 4-amino-furopyrimidines as Tie-2 and VEGFR2 dual inhibitors.Miyazaki Y., Matsunaga S., Tang J., Maeda Y., Nakano M., Philippe R.J., Shibahara M., Liu W., Sato H., Wang L., Nolte R.T.Bioorg. Med. Chem. Lett. 15:2203-2207(2005) Evolution of a highly selective and potent 2-(pyridin-2-yl) -1,3,5-triazine Tie-2 kinase inhibitor.Hodous B.L., Geuns-Meyer S.D., Hughes P.E., Albrecht B.K., Bellon S., Bready J., Caenepeel S., Cee V.J., Chaffee S.C., Coxon A., Emery M., Fretland J., Gallant P., Gu Y., Hoffman D., Johnson R.E., Kendall R., Kim J.L., Long A.M., Morrison M., Olivieri P.R., Patel V.F., Polverino A., Rose P., Tempest P., Wang L., Whittington D.A., Zhao H.J. Med. Chem. 50:611-626(2007) Design, synthesis, and biological evaluation of novel 3-aryl-4-(1H-indole-3yl) -1,5-dihydro-2H-pyrrole-2-ones as vascular endothelial growth factor receptor (VEGF-R) inhibitors.Peifer C., Selig R., Kinkel K., Ott D., Totzke F., Schaechtele C., Heidenreich R., Roecken M., Schollmeyer D., Laufer S.J. Med. Chem. 51:3814-3824(2008) Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling.Yang Y., Xie P., Opatowsky Y., Schlessinger J.Proc. Natl. Acad. Sci. U.S.A. 107:1906-1911(2010) Structural determinants of growth factor binding and specificity by VEGF receptor 2.Leppanen V.M., Prota A.E., Jeltsch M., Anisimov A., Kalkkinen N., Strandin T., Lankinen H., Goldman A., Ballmer-Hofer K., Alitalo K.Proc. Natl. Acad. Sci. U.S.A. 107:2425-2430(2010) The structural basis for the function of two anti-VEGF receptor 2 antibodies.Franklin M.C., Navarro E.C., Wang Y., Patel S., Singh P., Zhang Y., Persaud K., Bari A., Griffith H., Shen L., Balderes P., Kussie P.Structure 19:1097-1107(2011) Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma.Walter J.W., North P.E., Waner M., Mizeracki A., Blei F., Walker J.W.T., Reinisch J.F., Marchuk D.A.Genes Chromosomes Cancer 33:295-303(2002) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) Patterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) Suppressed NFAT-dependent VEGFR1 expression and constitutive VEGFR2 signaling in infantile hemangioma.Jinnin M., Medici D., Park L., Limaye N., Liu Y., Boscolo E., Bischoff J., Vikkula M., Boye E., Olsen B.R.Nat. Med. 14:1236-1246(2008) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of KDR recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for KDR purchase

MBS967496 is a recombinant protein targeting KDR. Also known as Recombinant Human Vascular endothelial growth factor receptor 2. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for KDR. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
UniProt Protein Name
Vascular endothelial growth factor receptor 2
UniProt Synonym Protein Names
Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; KDR; Protein-tyrosine kinase receptor flk-1; CD_antigen: CD309
UniProt Gene Name
KDR
UniProt Synonym Gene Names
FLK1; VEGFR2; VEGFR-2; FLK-1; KDR
UniProt Entry Name
VGFR2_HUMAN
NCBI Protein Information
vascular endothelial growth factor receptor 2

NCBI Summary for KDR

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]
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UniProt Comments for KDR

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.
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

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