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>   首页   >   产品   >   一抗   >   精选抗体   >   磷酸化抗体   >   Anti-WAVE2 (Tyr-150) [conserved site], Phosphospecific Antibody   

Anti-WAVE2 (Tyr-150) [conserved site], Phosphospecific Antibody

     
  • 1 - Anti-WAVE2 (Tyr-150) [conserved site], Phosphospecific Antibody AN2025
    Western blot of human K562 cells treated with pervanadate (1 mM, 30 min) (lanes 1 & 3) then treated with alkaline phosphatase (lanes 2 & 4). The blots were probed with anti-WAVE2 (Central region) (lanes 1 & 2) or anti-WAVE (Tyr-150) (lanes 3 & 4).
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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, ICC
Primary Accession Q9Y6W5
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 54284 Da
Additional Information
Gene ID 10163
Other Names Wiskott-Aldrich syndrome verproline, Scar2, WASF2
Dilution WB~~1:1000
ICC~~N/A
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-WAVE2 (Tyr-150) [conserved site], Phosphospecific 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

The Wiskott–Aldrich syndrome protein (WASP) family is involved in various pathways that regulate actin cytoskeletal organization. This family includes WASP, N-WASP, and three WAVE/SCAR isoforms, WAVE1, 2, and 3. WAVE proteins play key roles in actin-mediated cell events, such as membrane ruffling and lamellipodia formation. WAVEs contain an N-terminal WAVE homology domain, a basic domain, a Proline-rich region, and carboxy terminal verprolin, cofilin, and acidic (VCA) region. WAVEs are thought to act downstream of the Rac GTPase, connecting Rac activation to induction of Arp 2/3-mediated actin polymerization. Regulation of WAVE activity can occur through tyrosine phosphorylation. Src phosphorylation of WAVE1 at Tyr-125 enhances binding to the Arp2/3 complex, and is required for WAVE inhibition of Arp2/3-mediated stress fiber formation. By contrast, WAVE2 phosphorylation of Tyr-150 by Abl may enhance Arp2/3 complex actin nucleation and microspike formation in fibroblasts. Thus, site-specific tyrosine phosphorylation may be important for controlling specific activities of WAVE proteins.

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