Anti-α-Actinin 4 (N-terminal) Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O43707 |
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Reactivity | Bovine |
Host | Rabbit |
Clonality | Rabbit Polyclonal |
Isotype | IgG |
Calculated MW | 104854 Da |
Gene ID | 81 |
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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. |
Format | Antigen Affinity Purified |
Storage | Maintain 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. |
Precautions | Anti-α-Actinin 4 (N-terminal) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |

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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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