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>   首页   >   Anti-α-Actinin 4 (Tyr-4), Phosphospecific Antibody   

Anti-α-Actinin 4 (Tyr-4), Phosphospecific Antibody

     
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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 O43707
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 104854 Da
Additional Information
Gene ID 81
Other Names a-actinin 4, actinin alpha4
Target/Specificity α-Actinins are widely expressed cytoskeletal proteins that cross-link actin filaments through anti-parallel homodimers of the rod domains. Four α-actinin genes have been discovered in humans with α-actinin 1 and 4 being widely expressed in non-muscle cells. α-Actinins contain three conserved domains that include an N-terminal actin binding domain, four spectrin-like repeats in the central region, and a C-terminal calmodulin binding domain. α-Actinin cross-links the actin filament networks and associates the network to focal adhesion sites through binding of talin and vinculin. α-Actinin 1 is phosphorylated at Tyr-12 by FAK, while α-actinin 4 can be phosphorylated at Tyr-4 and Tyr-31 after EGF treatment. Tyr-4 and Tyr-31 phosphorylation inhibit actin binding and reduces actin-filament driven multi-nucleation in rat kidney cells. Thus, phosphorylation in α-actinins may be important for regulating actin binding and actin cytoskeletal remodeling.
Dilution WB~~1:1000
Format Antigen Affinity Purified
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-α-Actinin 4 (Tyr-4), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice

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

BACKGROUND

α-Actinins are widely expressed cytoskeletal proteins that cross-link actin filaments through anti-parallel homodimers of the rod domains. Four α-actinin genes have been discovered in humans with α-actinin 1 and 4 being widely expressed in non-muscle cells. α-Actinins contain three conserved domains that include an N-terminal actin binding domain, four spectrin-like repeats in the central region, and a C-terminal calmodulin binding domain. α-Actinin cross-links the actin filament networks and associates the network to focal adhesion sites through binding of talin and vinculin. α-Actinin 1 is phosphorylated at Tyr-12 by FAK, while α-actinin 4 can be phosphorylated at Tyr-4 and Tyr-31 after EGF treatment. Tyr-4 and Tyr-31 phosphorylation inhibit actin binding and reduces actin-filament driven multi-nucleation in rat kidney cells. Thus, phosphorylation in α-actinins may be important for regulating actin binding and actin cytoskeletal remodeling.

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