Alp-Actinin Pure 23/Alp-Actinin 50ug

α-Actinin is a member of a large family of actin-cross-linking proteins that includes fimbrin, dystrophin, and spectrin. α-Actinins form

homodimers composed of two polypeptide subunits arranged in an antiparallel orientation. The structure of α-Actinin 1 includes an N-terminal

actin-binding domain (ABD), four spectrin-like repeats, and two C-terminal EF hand motifs. A second smooth muscle isoform of α-Actinin 1

contains a single EF hand motif and is insensitive to calcium. Other homologous isoforms of α-Actinin include α-Actinin 4 cloned from a

tumor cell line, and two skeletal muscle isoforms, α-Actinin 2 and 3. In non-muscle cells α-Actinin colocalizes with actin and stabilizes the

actin filament web. The localization of α-Actinin in focal adhesion plaques suggests that it might serve to anchor the network of actin

filaments to the plasma membrane. Interestingly, Focal adhesion kinase (FAK) can phosphorylate α-Actinin at Tyr-12 and this may reduce its

binding capacity for actin filaments. α-Actinin interacts with several cytoskeletal proteins in addition to actin, including vinculin, zyxin,

palladin, and CLP-36. Thus, α-Actinin may be critical for mediating the interaction between actin filaments and various cytoskeletal proteins.

This antibody recognizes α-Actinin 1 and may recognize α-Actinin 4, however, it does not recognize α-Actinins found in skeletal muscle.

1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.

2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.