Product Pathways - Cytoskeletal Signaling
Phospho-Myosin IIa (Ser1943) Antibody #5026
|5026S||100 µl (10 western blots)||---||In Stock||---|
|5026||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||230||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-Myosin IIa (Ser1943) Antibody detects endogenous levels of myosin IIa protein only when phosphorylated at Ser1943.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser1943 of human myosin IIa protein. Antibodies are purified using protein A and peptide affinity chromatography.
Western blot analysis of extracts from HeLa, A-431 and 293T cells, untreated or treated with λ phosphatase and calf intestinal phosphatase (CIP), using Phospho-Myosin IIa (Ser1943) Antibody (upper) or Myosin IIa Antibody #3403 (lower).
Western blot analysis of extracts from A-431 cells, untreated or treated with λ phosphatase and calf intestinal phosphatase (CIP), using Phospho-Myosin IIa (Ser1943) Antibody. The antibody was pre-incubated with peptides corresponding to unphosphorylated Myosin IIa or Myosin IIa phosphorylated at Ser1943, as indicated.
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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