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PEDS Advance Access originally published online on July 22, 2009
Protein Engineering Design and Selection 2009 22(10):625-629; doi:10.1093/protein/gzp046
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© The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Tubulin isotype specificity and identification of the epitope for antibody Tub 2.1

Hailing Yang, Fernando Cabral and Rajat Bhattacharya1

Department of Integrative Biology and Pharmacology, The University of Texas Medical School, Houston, TX 77030, USA

1 To whom correspondence should be addressed. E-mail: rajat.bhattacharya{at}uth.tmc.edu or rajatbhatt{at}mail.com

Tub 2.1, a monoclonal antibody commonly used to measure cellular tubulin content, is widely believed to recognize all β-tubulin isotypes. Though it has been used for more than two decades, the epitope for this antibody is not well established. We report for the first time that contrary to common belief, this antibody does not react with all isotypes of β-tubulin. Of the seven vertebrate β-tubulins, the more divergent class V and VI isotypes are not recognized by this antibody. Among the isotypes that do react, binding is similar for β2, β3, β4a and β4b but lower for β1, the most abundant isotype. Expression of chimeric tubulins verified that the epitope for Tub 2.1 is near the C-terminal end of β-tubulin. Site-directed mutagenesis of this region in nonreactive β5 to match the sequence of β4b resulted in strong reaction to Tub 2.1 and narrowed the epitope to amino acids 431–436.

Keywords: multiple tubulin isotypes/pan specific antibody/variable reactivity

Received February 3, 2009; revised June 8, 2009; accepted June 30, 2009.


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