Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Myosin VI Antibody #9200

Applications Reactivity Sensitivity MW (kDa) Source
W H Dg Endogenous 150 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Myosin VI Antibody recognizes endogenous levels of total myosin VI protein. Based on sequence homology, the antibody is expected to detect all isoforms of myosin VI.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human myosin VI protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Myosin VI Antibody.

Background

The myosin family of motor proteins drive ATP-dependent actin-based motility in eukaryotic cells and contain a conserved amino-terminal motor domain (reviewed in 1,2).Myosin VI is an unconventional minus-end-directed myosin involved in the transport of vesicles and organelles within the cell, endocytosis, and organelle biogenesis (3-6). The movement of myosin VI and its cargo along actin filaments is unique among myosin family members in its mechanism; its tail domain structure allows it to take larger than predicted steps along the actin filament (reviewed in 1,7).Myosin VI has been shown to regulate the polarized delivery of proteins to specialized subcellular locations, including the delivery of EGFR to the leading edge of migrating cells (8), as well as the delivery of specialized axonal proteins in neurons (9). Myosin VI has also been shown to mediate activity of the tumor suppressor p53 during DNA damage (10,11).

  1. Sweeney, H.L. and Houdusse, A. (2010) Cell 141, 573-82.
  2. Nambiar, R. et al. (2010) Cell Mol Life Sci 67, 1239-54.
  3. Bond, L.M. et al. (2011) Mol Biol Cell 22, 54-65.
  4. Aschenbrenner, L. et al. (2004) Mol Biol Cell 15, 2253-63.
  5. Loubéry, S. et al. (2012) Traffic 13, 665-80.
  6. Ameen, N. and Apodaca, G. (2007) Traffic 8, 998-1006.
  7. Spudich, J.A. and Sivaramakrishnan, S. (2010) Nat Rev Mol Cell Biol 11, 128-37.
  8. Chibalina, M.V. et al. (2010) Traffic 11, 1290-303.
  9. Lewis, T.L. et al. (2011) PLoS Biol 9, e1001021.
  10. Jung, E.J. et al. (2006) Mol Cell Biol 26, 2175-86.
  11. Cho, S.J. and Chen, X. (2010) J Biol Chem 285, 27159-66.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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