Myosin Light Chain 2 Antibody Sampler Kit #9776
Product Information
Kit Usage Information
Protocols
- 3671: Western Blotting, Immunofluorescence
- 3674: Western Blotting
- 7074: Western Blotting
- 8505: Western Blotting
Product Description
The Myosin Light Chain 2 Antibody Sampler Kit provides an economical means to detect total, phosphorylated, and dual-phosphorylated myosin light chain 2. The kit contains enough primary and secondary antibody to perform two western blot experiments.
Specificity / Sensitivity
The antibodies in the Myosin Light Chain 2 Antibody Sampler Kit detect endogenous levels of total myosin light chain 2 (smooth muscle), myosin light chain 2 when phosphorylated at Ser19 or when dually phosphorylated at Thr18 and Ser19, respectively. The antibodies do not cross-react with the cardiac isoform of Myosin Light Chain 2.
Source / Purification
The rabbit monoclonal antibody is produced by immunizing rabbits with a synthetic peptide corresponding to residues near the carboxy terminus of human myosin light chain 2 protein. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser19 of human myosin light chain 2, or to residues surrounding Thr18/Ser19 of human myosin light chain 2, respectively. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
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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For Research Use Only. Not For Use In Diagnostic Procedures.
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