R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Phospho-Myosin IIa (Ser1943) (D7Z7T) Rabbit mAb #14611
Filter:
- WB
- IF
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 230 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Phospho-Myosin IIa (Ser1943) (D7Z7T) Rabbit mAb recognizes endogenous levels of myosin IIa protein only when phosphorylated at Ser1943.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser1943 of human myosin II protein.
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).
- 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.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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