Description

Background:

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]

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.

Product datasheet:

Overview

Product Description   Phospho-Flk-1 (Y1214) Polyclonal Antibody, 100µg, (ATB-P0111)
Image
Species ReactivitiesHuman,Mouse,Rat
ImmunogenSynthesized peptide derived from human Flk-1 around the phosphorylation site of Y1214.

Properties

FormLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions-20°C/1 year
ClonalityPolyclonal

References:

  1. Inverse correlation of phospho-KDR/Flk-1 expression and stage of colorectal cancer: implication of the significance of neoangiogenesis in activated VEGFR-2 expressing early stage colorectal adenocarcinomas. Lin YF, et al. Pol J Pathol, 2014 Oct. PMID 25372416
  2. Regulatory roles of KDR antisense oligonucleotide on the proliferation of human prostate cancer cell line PC-3. Song J, et al. J BUON, 2014 Jul-Sep. PMID 25261665
  3. Functional and structural characterization of the kinase insert and the carboxy terminal domain in VEGF receptor 2 activation. Manni S, et al. FASEB J, 2014 Nov. PMID 25114179
  4. Dioscin inhibits colon tumor growth and tumor angiogenesis through regulating VEGFR2 and AKT/MAPK signaling pathways. Tong Q, et al. Toxicol Appl Pharmacol, 2014 Dec 1. PMID 25111127
  5. Kinase insert domain receptor/vascular endothelial growth factor receptor 2 (KDR) genetic variation is associated with ovarian hyperstimulation syndrome. O’Brien TJ, et al. Reprod Biol Endocrinol, 2014 May 9. PMID 24886133 Free PMC Article
  6. 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) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH VEGFC, SUBCELLULAR LOCATION.
  7. 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) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INHIBITION OF LYMPHANGIOGENESIS, INTERACTION WITH VEGFC, TISSUE SPECIFICITY.

  8. Full length human KDR/flk-1 sequence.
    Yin L.Y., Wu Y., Patterson C.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  9. Coding region for human VEGF receptor KDR (VEGFR-2).
    Yu Y., Whitney R.G., Sato J.D.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Umbilical vein.
  10. 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) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

external
sizechest(in.)waist(in.)hips(in.)
XS34-3627-2934.5-36.5
S36-3829-3136.5-38.5
M38-4031-3338.5-40.5
L40-4233-3640.5-43.5
XL42-4536-4043.5-47.5
XXL45-4840-4447.5-51.5

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