Product Pathways - Cytoskeletal Signaling
Myosin IIb Antibody #3404
|3404S||100 µl (10 western blots)||---||In Stock||---|
|3404||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Monkey||Endogenous||230||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry)
Species predicted to react based on 100% sequence homology: Rat.
Specificity / Sensitivity
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.
Western blot analysis of extracts from COS cells, untransfected or transfected with nonmuscle EGFP-myosin IIa, IIb or IIc, using Myosin IIb Antibody.
Western blot analysis of extracts from various cell types using Myosin IIb Antibody.
Confocal immunofluorescent analysis of Cos cells using Myosin IIb Antibody (green). Actin filaments have been labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).
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). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).
- Conti, M.A. and Adelstein, R.S. (2008) J Cell Sci 121, 11-18.
- Sandquist, J.C. et al. (2006) J Biol Chem 281, 35873-83.
- Even-Ram, S. et al. (2007) Nat Cell Biol 9, 299-309.
- Vicente-Manzanares, M. et al. (2007) J Cell Biol 176, 573-80.
- Wylie, S.R. and Chantler, P.D. (2008) Mol Biol Cell 19, 3956-68.
- Sandquist, J.C. and Means, A.R. (2008) Mol Biol Cell 19, 5156-67.
- Dulyaninova, N.G. et al. (2007) Mol Biol Cell 18, 3144-55.
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