alpha-Actinin 4 Phospho-Regulation Antibody Sampler Kit

Background:
α-Actinins are widely expressed cytoskeletal proteins that cross-link actin filaments through antiparallel 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 inhibits actin binding and reduces actin-filament driven multinucleation in rat kidney cells. Thus, phosphorylation in α-actinins may be important for regulating actin binding and actin cytoskeletal remodeling.

Buffer/Storage:
Mouse monoclonal and rabbit polyclonal antibodies are supplied in phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. The secondary reagents are supplied in the same buffer without azide. Store all at –20°C. Stable for 1 year.

Product References:
AP4241 Kojima, S. et al. (2014) Am J Nephrol. 39(1):36-45 WB: human kidney cells
AP4271 Kojima, S. et al. (2014) Am J Nephrol. 39(1):36-45 WB: human kidney cells
RS3251 Kawasaki, H. et al. (2013) World J Gastroenter. 19(17):2629. WB, ICC: mouse intestinal myofibroblasts
MS3001 Estrada-Bernal, A. et al. (2011) J Neurooncol. 102:353. Western Blot
RS3251 Estrada-Bernal, A. et al. (2011) J Neurooncol. 102:353. Western Blot