Phospho-Myosin Light Chain 2 (Ser19) Mouse mAb #3675
Filter:
- WB
- IF
Supporting Data
| REACTIVITY | H M R B Pg |
| SENSITIVITY | Endogenous |
| MW (kDa) | 18 |
| Source/Isotype | Mouse IgG1 |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- B-Bovine
- Pg-Pig
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:10 - 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:200 - 1:400 |
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 Light Chain 2 (Ser19) Mouse mAb detects endogenous levels of myosin light chain 2 (smooth muscle) only when phosphorylated at serine 19. This antibody does not cross-react with the cardiac isoform of myosin light chain 2.
Species Reactivity:
Human, Mouse, Rat, Bovine, Pig
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser19 of human myosine light chain 2 (smooth muscle).
Background
Myosin is composed of six polypeptide chains: two identical heavy chains and two pairs of light chains. Myosin light chain 2 (MLC2), also known as myosin regulatory light chain (MRLC), RLC, or LC20, has many isoforms depending on its distribution. In smooth muscle, MLC2 is phosphorylated at Thr18 and Ser19 by myosin light chain kinase (MLCK) in a Ca2+/calmodulin-dependent manner (1). This phosphorylation is correlated with myosin ATPase activity and smooth muscle contraction (2). ROCK also phosphorylates Ser19 of smooth muscle MLC2, which regulates the assembly of stress fibers (3). Phosphorylation of smooth muscle MLC2 at Ser1/Ser2 and Ser9 by PKC and cdc2 has been reported to inhibit myosin ATPase activity (4,5). Phosphorylation by cdc2 controls the timing of cytokinesis (5). Transgenic mice lacking phosphorylation sites on the cardiac muscle isoform show morphological and functional abnormalities (6).
- Ikebe, M. and Hartshorne, D.J. (1985) J. Biol. Chem. 260, 10027-10031.
- Tan, J. L. et al. (1992) Annu. Rev. Biochem. 61, 721-759.
- Totsukawa, G. et al. (2000) J. Cell Biol. 150, 797-806.
- Ikebe, M. et al. (2000) J. Biol. Chem. 262, 9569-9573.
- Satterwhite, L. L. et al. (1992) J. Cell Biol. 118, 595-605.
- Sanbe, A. et al. (1999) J. Biol. Chem. 274, 21085-21094.
限制使用
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