Abstract
Glucose-regulated protein (GRP78), an ER chaperone that belongs to the heat-shock protein (HSP) family, exist in all cells and plays important roles in maintaining cellular homeostasis. GRP78 participates in protein folding, transportation, and degradation. Lack of high affinity antibodies especially monoclonal antibodies (MAbs) suitable for Western blot and immunohistochemical staining has lagged. To gain further insight into its possible functions, we generated a novel MAb specific for hGRP78 in Western blot and immunohistochemistry and localized hGRP78 in some human cancer cell lines and cancer tissues. Immunoreactivity of GRP78 was prominent in Hela, Colo205, and A549 detected by 3F9 in Western blot analysis. 3F9 antibody recognized endogenous GRP78 in human cervical cancer, colonic cancer, esophageal cancer, and lung cancer. Thus, successful production of GRP78 monoclonal antibodies provides a new powerful tool for investigation of GRP78 function.
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