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Item No. 35807
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Detyrosinated α-tubulin is a form of the cytoskeletal protein α-tubulin that has been post-translationally modified by the tubulin carboxypeptidases vasohibin 1 (VASH-1) and VASH-2, which remove the C-terminal tyrosine from α-tubulin.1 Detyrosination of α-tubulin occurs in the cytosol and exposes two consecutive glutamate residues that can be further processed to form Δ2- or Δ3-tubulin. Detyrosinated α-tubulin monomers can be re-tyrosinated by tubulin tyrosine ligase and be incorporated into microtubules again. α-Tubulin detyrosination is associated with, but not sufficient for, increased stability of the microtubule and is involved in a variety of biological processes, including neuronal development, β-oxidation, mitosis, and cardiomyocyte contraction.2,3,1,4 Increased levels of detyrosination are associated with tumor development in vitro, have been found in tumor tissue from patients with breast cancer, and are positively correlated with breast cancer aggressiveness.5,6 Cayman’s Detyrosinated α-Tubulin Rabbit Monoclonal Antibody (Clone RM444) can be used for immunocytochemistry (ICC), immunofluorescence (IF), and Western blot (WB) applications.
WARNING This product is not for human or veterinary use.
1. The tubulin detyrosination cycle: Function and enzymes. Trends Cell Biol. 29(1), 80-92 (2019).
2. α-
3. AMPK activation promotes lipid droplet dispersion on detyrosinated microtubules to increase mitochondrial fatty acid oxidation. Nat. Commun. 6, 7176 (2015).
4. Suppression of detyrosinated microtubules improves cardiomyocyte function in human heart failure. Nat. Med. 24(8), 1225-1233 (2018).
5. Post-
6. Tubulin detyrosination is a frequent occurrence in breast cancers of poor prognosis. Cancer Res. 61(13), 5024-5027 (2001).