|Tested applications||WB IHC|
|Recommended Dilution||WB 1:1000 - 1:2000
IHC 1:50 - 1:100|
|Observed MW||Refer to Figures|
|Immunogen||Recombinant protein of human MYH9|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
|Synonym||MYH9;DFNA17;EPSTS;FTNS;MGC104539;MHA;NMHC-II-A;NMMHCA ; Myosin Iia;|
Western blot analysis of extracts of various cells, using MYH9 antibody.
Immunohistochemistry of paraffin-embedded human esophagus using MYH9 antibody at dilution of 1:100 (40x lens).
Immunohistochemistry of paraffin-embedded human stomach using MYH9 antibody at dilution of 1:100 (40x lens).
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). Phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).
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