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Anti-VEGFR-3 (N-terminus) Antibody

     
  • 1 - Anti-VEGFR-3 (N-terminus) Antibody AN2015
    Left: Western blot image of human K-562 cells (lanes 1 & 2) and HUVEC (lanes 3 & 4). The blots were probed with rabbit polyclonal anti-VEGFR-3 (a.a. 1285-1298) in the absence (lanes 1 & 3) or presence of blocking peptide (VX2945) (lanes 2 & 4). Right: Western blot image of GST-recombinant human VEGFR-1 (89 kDa), VEGFR-2 (110 kDa), and VEGFR-3 (86 kDa) C-terminal regions. The blot was probed with anti-VEGFR-3 (a.a. 1285-1298).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P35916
Reactivity Rat
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 152757 Da
Additional Information
Gene ID 2324
Other Names FLT-4, Vascular endothelial growth factor receptor 3
Dilution WB~~1:1000
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-VEGFR-3 (N-terminus) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Vascular endothelial growth factor receptor-2 (VEGFR-2/Flk-1/KDR) is the primary receptor for VEGF in endothelial cells. Other VEGFR family members, VEGFR-1 (Flt-1) and VEGFR-3 (Flt-4), can also transduce the intracellular signals of VEGF. However, the role of VEGFR-1 is observed mainly during embryonic angiogenesis and VEGFR-3 signaling may be restricted to specific types of endothelial cells. Major autophosphorylation sites of VEGFR-2 are located in the kinase insert domain (Tyr-951/996) and in the tyrosine kinase catalytic domain (Tyr-1054/1059). Other sites, Tyr-1175 and Tyr-1212 provide docking sites for downstream signaling molecules. Activation of VEGFR-2 also phosphorylates Tyr-801, leading to PI3-kinase-Akt activation and increases in endothelial nitric oxide synthase activity. Phosphorylation of mutliple sites in VEGFR-2 is required for downstream activation of several signaling pathways that control proliferation, chemotaxis, and sprouting during angiogenesis.

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