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Anti-Vav3 Antibody

     
  • 1 - Anti-Vav3 Antibody AN2012
    Western blot of human Jurkat (lanes 1 & 4), HUVEC (lanes 2 & 5), and A431 (lanes 3 & 6) cells. The blots were probed with anti-Vav2 (a.a. 309-322) at a dilution of 1:500 (lanes 1-3) and anti-Vav3 (a.a. 293-305) at 1:500 (lanes 4-6).
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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 Q9UKW4
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 97776 Da
Additional Information
Gene ID 10451
Other Names VAV3, Guanine nucleotide exchange factor VAV3
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-Vav3 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 Vav family of Rho-guanine nucleotide exchange factors, Vav1, Vav2, and Vav3, have central roles in transducing signals from cell surface receptors, such as integrin, growth factor and immune cell receptors to the cytoskeleton. This role includes receptor-mediated changes in the actin cytoskeleton and cell motility. Vav1 expression is normally restricted to hematopoietic cells, while Vav2 and Vav3 are more widely expressed. All three Vav isoforms have been shown to be abnormally expressed in several types of cancer. Vavs are composed of multiple domains, including a Dbl homology domain, a calponin homology domain, an acidic amino acid region, a pleckstrin homology domain, a cysteine-rich domain, and SH3 and SH2 domains. Vav activity is regulated by the phosphorylation status of several conserved tyrosine residues in the acidic region (In Vav2: Tyr-142, Tyr-159, and Tyr-172). These tyrosine residues are able to participate in autoinhibitory interactions with the Dbl homology domain and this interaction is prevented after phosphorylation of these sites leading to activation of Vav GEF activity.

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