The Acetyl-α-Tubulin (Lys40) antibody specifically detects α-tubulin acetylated at lysine residue 40. a post-translational modification occurring in microtubules. α-Tubulin, a core component of microtubules, undergoes acetylation via α-tubulin acetyltransferase (ATAT1), which stabilizes microtubule structure by reducing protofilament flexibility and enhancing resistance to mechanical stress. Lys40 acetylation is enriched in long-lived, stable microtubules, such as those in cilia, axons, and mitotic spindles, and is associated with cellular processes like intracellular trafficking, cell motility, and polarization.
This antibody is widely used to study microtubule dynamics and their roles in cellular physiology or disease. It serves as a marker for assessing microtubule stability in conditions like cancer (e.g., metastatic progression linked to altered microtubule acetylation) or neurodegenerative disorders (e.g., impaired axonal transport). Researchers employ it in techniques including Western blotting, immunofluorescence, and immunohistochemistry to visualize acetylated microtubules in cells, tissues, or model organisms.
The specificity of the antibody is critical, as improper validation may lead to cross-reactivity with unrelated acetylated epitopes. Controls, such as comparing treated vs. untreated samples (e.g., using deacetylase inhibitors like trichostatin A) or genetic models lacking ATAT1. are essential to confirm signal accuracy. Its applications span basic research in cell biology, screening for microtubule-targeting drugs, and exploring therapeutic strategies for diseases involving microtubule dysfunction.