Open AccessGeneration and Characterization of Mouse Monoclonal Antibodies Against CIP75, an UbL-UBA Domain-containing Protein
Author(s) -
Vivian Su,
Andrew Kekūpaʻa Knutson,
Katharine Lau,
Wendy E. Kurata,
John M. Berestecky,
Alan F. Lau
Publication year - 2009
Publication title -
hybridoma
Language(s) - English
Resource type - Journals
eISSN - 1557-8348
pISSN - 1554-0014
DOI - 10.1089/hyb.2008.0082
Subject(s) - immunoprecipitation , monoclonal antibody , ubiquitin , immunofluorescence , microbiology and biotechnology , antibody , protein degradation , intracellular , blot , chemistry , biology , biochemistry , immunology , gene
CIP75 is a member of the UbL(ubiquitin-like)-UBA (ubiquitin-associated) domain containing protein family, which has a variety of functions. One specific role described for several members of the UbL-UBA family is the involvement in the proteasomal degradation of target proteins. We have reported that CIP75 interacts with the gap junction protein, connexin43 (Cx43), and that CIP75 may modulate the proteasomal degradation of Cx43. Thus, CIP75 may have a critical role in regulating Cx43 levels, and thus intercellular gap junctional communication. This study reports the development of monoclonal antibodies (MAbs) against CIP75 and the characterization of these antibodies through immunoblotting, immunoprecipitation, and immunofluorescence microscopy analyses. These MAbs will be useful tools in future studies to elucidate the role of CIP75 in Cx43 proteasomal degradation as well as other potential activities.