Myosins belong to a superfamily of actin-based motor proteins comprising to date at least 15 classes. Myosin I (also designated myosin-1c, myo1c, M1C, myr 2 and myh 2) is a widely distributed single-headed myosin composed of an N-terminal motor domain, a calmodulin-light chain binding neck region, and a short C-terminal domain. In mammalian cells, myosin I is usually found in the cytoplasm and is especially enriched in perinuclear regions and dynamic cell margins. Myosin Iβ is found in a variety of cells such as kidney tubular cells and inner-ear hair cells.

Recognizes the heavy chain of the nuclear form of human myosin Iβ. Additional bands may be detected in some preparations.

synthetic peptide corresponding to amino acid residues 1-16 of the heavy chain of mouse myosin Iβ (nuclear form). This sequence is missing from the other myosin I isoforms as well as from other currently known myosins.

Anti-Myosin Iβ (Nuclear) antibody produced in rabbit has been used in:

• western blot
• confocal immunofluorescence
• immunogold labeling
• immunofluorescence
• co-immunoprecipitation experiments
• immunostaining

Myosin I is involved in cell motility, microvilli anchorage, vesicular and organelle transport and signal transduction. Myosin I associate with lipid membranes through its tail domain while its motor domain interacts with actin filaments. Myosin Iβ (nuclear) co-localizes with RNA polymerases I and II and possibly acts as a molecular motor to power transcription.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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