Revision 1

#9776Store at -20C

1 Kit

(3 x 20 microliters)

Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

Support: 877-678-TECH (8324)

Web: [email protected] cellsignal.com

3 Trask LaneDanversMassachusetts01923USA
For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
Phospho-Myosin Light Chain 2 (Ser19) Antibody 3671 20 µl 18 kDa Rabbit 
Phospho-Myosin Light Chain 2 (Thr18/Ser19) Antibody 3674 20 µl 18 kDa Rabbit 
Myosin Light Chain 2 (D18E2) Rabbit mAb 8505 20 µl 18 kDa Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

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.

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.

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).

  1. Ikebe, M. and Hartshorne, D.J. (1985) J. Biol. Chem. 260, 10027-10031.
  2. Tan, J. L. et al. (1992) Annu. Rev. Biochem. 61, 721-759.
  3. Totsukawa, G. et al. (2000) J. Cell Biol. 150, 797-806.
  4. Ikebe, M. et al. (2000) J. Biol. Chem. 262, 9569-9573.
  5. Satterwhite, L. L. et al. (1992) J. Cell Biol. 118, 595-605.
  6. Sanbe, A. et al. (1999) J. Biol. Chem. 274, 21085-21094.

Background References

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    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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