α-Tubulin K40Ac Rabbit Monoclonal Antibody (Clone RM318)

α-Tubulin is a cytoskeletal protein and constituent of microtubules, a cytoskeletal assembly that has roles in a variety of cellular processes, including cell motility, division, differentiation, and intracellular transport.¹ α-Tubulin is highly conserved in eukaryotes and expressed in a cell- and isotype-specific manner.² There are eight human α-tubulin isotypes that consist of an N-terminal domain, which binds GTP and is required for microtubule self-assembly, and a variable C-terminal tail, which contains interaction sites for microtubule-associated proteins (MAPs) and is subject to a variety of post-translational modifications that regulate microtubule function and stability.^3,4,1,5 α-Tubulin can be acetylated at a variety of sites, including on the luminal side of microtubules at lysine 40 (K40Ac), by α-tubulin N-acetyltransferase 1 (α-TAT) and deacetylated primarily by histone deacetylase 6 (HDAC6).^6,7 α-Tubulin K40Ac is a marker of stable microtubules that recruits dynein and kinesin-1 to microtubules. It is also involved in regulating microtubule architecture as well as immune and viral responses.^6,8,7 The levels of α-tubulin acetylation are decreased in a variety of neurological disorders, increased in various cancers, and dysregulated in immune disorders.⁷ Cayman’s α-Tubulin K40Ac Rabbit Monoclonal Antibody (Clone RM318) can be used for immunocytochemistry (ICC) and Western blot (WB) applications.

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1. Gadadhar, S., Bodakuntla, S., Natarajan, K., et al. The tubulin code at a glance. J. Cell Sci. 130(8), 1347-1353 (2017).

2. Binarová, P., and Tuszynski, J. Tubulin: Structure, functions and roles in disease. Cells 8(10), 1294 (2019).

3. Vemu, A., Atherton, J., Spector, J.O., et al. Tubulin isoform composition tunes microtubule dynamics. Mol. Biol. Cell 28(25), 3564-3572 (2017).

4. Valiron, O. New insights into microtubule elongation mechanisms. Commun. Integr. Biol. 4(1), 10-13 (2011).

5. Zhang, F., Su, B., Wang, C., et al. Posttranslational modifications of α-tubulin in Alzheimer disease. Transl. Neurodegener. 4(9), (2015).

6. Sadoul, K., and Khochbin, S. The growing landscape of tubulin acetylation: Lysine 40 and many more. Biochem. J. 473(13), 1859-1868 (2016).

7. Li, L., and Yang, X.-J. Tubulin acetylation: Responsible enzymes, biological functions and human diseases. Cell. Mol. Life Sci. 72(22), 4237-4255 (2015).

8. Dompierre, J.P., Godin, J.D., Charrin, B.C., et al. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington’s disease by increasing tubulin acetylation. J. Neurosci. 27(13), 3571-3583 (2007).