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

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.

Our α-Actinin 4 (Tyr-4) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat α-Actinin 4 (Tyr-4) and is antigen affinity purified. It is great for use in WB.

Phospho-α-actinin 4 (Tyr-4) synthetic peptide (coupled to carrier protein) corresponding to amino acids in the N-terminus of human α-actinin 4. This sequence is well conserved in rat and mouse α-actinin 4, but is not conserved in other α-actinins.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects a 100 kDa* protein corresponding to the molecular mass of α-actinin 4 on SDS-PAGE immunoblots of human A431 cells treated with pervanadate, but is not observed after akaline phosphatase treatment.