Anti-acetyl-alpha tubulin Antibody, clone 6-11B-1 clone 6-11B-1, from mouse

Microtubules are cytoskeletal filaments composed of of alpha-/beta-tubulin heterodimers that self-assemble head-to-tail to form protofilaments and laterally to form a hollow tube. Various post-translational modifications (PTMs), including acetylation, polyglutamylation, polyglycylation, detyrosination, phosphorylation, and palmitoylation, can regulate the polymerization properties of tubulins and/or their interactions with microtubule associated proteins (MAPs) and motor proteins. A subset of cytoplasmic microtubules and microtubules in the spindle, axon, and cilia are known to contain alpha-tubulin acetylated via the epsilon-amino group of Lysine-40 (K40). The GNAT lysine acetyltransferase family member MEC-17 (or alpha-tubulin acetyltransferase/alphaTAT) catalyzes K40 acetylation, while HDAC6 and sirtuin2 (SIRT2) are known to catalyze tubulin deacetylation. Experimental evidences indicate that K40 acetylation primes alpha-tubulin for further PTM(s), which cannot be reversed by later deactylation of K40ac. Subsequently, the acetylated and deacetylated alpha-tubulin in native microtubules are structurally distinct from that of unacetylated alpha-tubulin (never before has its K40 acetylated).