Myosin IIb Antibody detects endogenous levels of total myosin IIb protein. The antibody does not cross-react with the nonmuscle heavy chains of myosin IIa or IIc.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human myosin IIb.
Background
Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).