Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - Cytoskeletal Signaling

Myosin IIb (D8H8) XP® Rabbit mAb #8824

Applications Reactivity Sensitivity MW (kDa) Isotype
W IF-IC H M R Mk Endogenous 230 Rabbit IgG

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Myosin IIb (D8H8) XP® Rabbit mAb recognizes endogenous levels of total myosin IIb protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human myosin IIb protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using Myosin IIb (D8H8) XP® Rabbit mAb.

IF-IC

IF-IC

Confocal immunofluorescent analysis of COS-7 cells using Myosin IIb (D8H8) XP® Rabbit mAb (green). Actin filaments were labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

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). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

  1. Conti, M.A. and Adelstein, R.S. (2008) J Cell Sci 121, 11-18.
  2. Sandquist, J.C. et al. (2006) J Biol Chem 281, 35873-83.
  3. Even-Ram, S. et al. (2007) Nat Cell Biol 9, 299-309.
  4. Vicente-Manzanares, M. et al. (2007) J Cell Biol 176, 573-80.
  5. Wylie, S.R. and Chantler, P.D. (2008) Mol Biol Cell 19, 3956-68.
  6. Sandquist, J.C. and Means, A.R. (2008) Mol Biol Cell 19, 5156-67.
  7. Dulyaninova, N.G. et al. (2007) Mol Biol Cell 18, 3144-55.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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