Actin is a major cytoskeletal protein involved in diverse cellular functions including cell motility, adhesion, and morphology. Six different actin isoforms have been identified in vertebrates. There are four α isoforms: skeletal, cardiac, and two smooth muscle (enteric and aortic) actins, along with two cytoplasmic actins (β and γ). Actin exists in two principal forms, globular, monomeric (G) actin, and filamentous polymeric (F) actin. The assembly and disassembly of actin filaments, and also their organization into functional networks, is regulated by a variety of actin-binding proteins (ABPs). Phosphorylation may also be important for regulating actin assembly and interaction with ABPs. In Dictyostelium, phosphorylation of Tyr-53 occurs in response to cell stress and this phosphorylation may alter actin polymerization. In B cells, SHP-1 tyrosine dephosphorylation of actin leads to actin filament depolymerization following BCR stimulation.
References
Western blot analysis of human HUVEC-CS (lane 1), rabbit spleen fibroblast (lane 2), human Jurkat (lane 3), human LNCaP (lane 4), human HeLa (lane 5), and mouse F9 (lane 6) cell lysates. The blot was probed with mouse monoclonal anti-β-Actin (AM0081) at 1:1000 (lanes 1-6).
Immunocytochemical labeling of β-Actin in paraformaldehyde fixed human MeWo cells. The cells were labeled with mouse monoclonal anti-β-Actin (clone M008). The antibody was detected using goat anti-mouse DyLight® 594.
*For more information, see UniProt Accession P60709
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
This kit contains:
