Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

γ-Tubulin Antibody #5886

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk Endogenous 50 Rabbit

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

Protocols

Specificity / Sensitivity

γ-Tubulin Antibody recognizes endogenous levels of total γ-tubulin protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human γ-tubulin 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 γ-Tubulin Antibody.

Background

Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. As a critical part of the microtubule-organizing center (MTOC), the third member of the tubulin superfamily, γ-tubulin, is required for microtubule nucleation as well as centrosome duplication and spindle assembly (1,2, reviewed in 3). γ-tubulin forms complexes of two different sizes: γ-tubulin small complex (γ-TuSC) and the larger γ-tubulin ring complex (γ-TuRC). Each complex consists of a number of γ-tubulin complex proteins (GCPs) with γ-tubulin itself being considered GCP1. GCP2-6 all share sequence similarity in 5 different regions and it is thought that these areas could play a role in the proper folding of the proteins (4). γ-TuSC is composed of two γ-tubulin molecules as well as GCP2 and GCP3. γ-TuRC is made up of a ring of multiple copies of γ-TuSC in addition to GCP4, 5, and 6. Another protein, GCP-WD/NEDD1, which lacks sequence similarity with the other GCPs, associates with the γ-TuRC. GCP-WD/NEDD1 has been shown to regulate localization of the γ-TuSC to spindles and centrosomes (5-8). In mammals, phosphorylation of γ-tubulin at Ser131 by SADB controls the activity of the γ-TuRC. The hypothesis is that this phosphorylation stabilizes the protein in a conformation that stimulates centrosome amplification (9).

  1. Westermann, S. and Weber, K. (2003) Nat Rev Mol Cell Biol 4, 938-47.
  2. Loncarek, J. and Khodjakov, A. (2009) Mol Cells 27, 135-42.
  3. Wiese, C. and Zheng, Y. (2006) J Cell Sci 119, 4143-53.
  4. Murphy, S.M. et al. (2001) Mol Biol Cell 12, 3340-52.
  5. Raynaud-Messina, B. and Merdes, A. (2007) Curr Opin Cell Biol 19, 24-30.
  6. Schiebel, E. (2000) Curr Opin Cell Biol 12, 113-8.
  7. Lüders, J. et al. (2006) Nat Cell Biol 8, 137-47.
  8. Haren, L. et al. (2009) PLoS One 4, e5976.
  9. Alvarado-Kristensson, M. et al. (2009) Nat Cell Biol 11, 1081-92.

Application References

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Companion Products

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

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