Date of Award


Publication Type

Master Thesis

Degree Name



Biological Sciences

First Advisor

Hubberstey, A.


Biology, Cell.



Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.


Human BAT3 is a 120kDa protein containing a large number of proline, glycine and charged amino acids. Human BAT3 has recently been shown to share 57% amino acid identity with the Xenopus Scythe protein, a regulator of Reaper-induced apoptosis. Due to this high degree of conservation, BAT3 may play a role in mammalian cell death. We have investigated the subcellular localization of human BAT3 by generating a fusion protein between the hemagglutinin (HA) epitope-tag and the full-length BAT3 protein. Using immunofluorescence microscopy and confocal imaging, we have found that full-length BAT3 is predominantly expressed in the nucleus, however a small percentage (10%) of cells exhibit cytoplasmic localization. We have constructed a series of deletion mutants fused to the HA-epitope tag and have over-expressed these proteins in HeLa cells. Immunofluorescent detection reveals that the expression of the amino terminal 656 amino acid residues results in strict cytoplasmic localization of BAT3. (Abstract shortened by UMI.)Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis2001 .M35. Source: Masters Abstracts International, Volume: 40-03, page: 0640. Adviser: Andrew Hubberstey. Thesis (M.Sc.)--University of Windsor (Canada), 2001.