This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Immunology and Nuclear Signaling research. In general, myosins are protein complexes consisting of one or more myosin heavy chains, associated light chains and other proteins. Myosins function as molecular motors and use the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments. Myosins have magnesium-ATPase activity and bind actin. Myosins can be divided into classes that are distinguished based on sequence features of the motor, or head domain, but also have distinct tail regions that are believed to bind specific cargoes. Unconventional myosins exist. Myosin 1G is an unconventional myosin that is restricted to hematopoietic cells. Unconventional myosins are also critical for motility in amoeba and a mammalian paralog (Myo1C) is critical as a glucose transporter that recycles glucose in response to insulin.
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to an internal region of human Myosin 1G protein.