The TRIP11 (Thyroid Hormone Receptor Interactor 11) antibody is a tool used to study the TRIP11 protein, also known as Golgi-associated PDZ and Coiled-coil Motif Containing Protein (GOPC). TRIP11 is a multi-domain scaffold protein involved in intracellular trafficking, Golgi apparatus organization, and vesicle-mediated transport. It contains PDZ, coiled-coil, and proline-rich domains, enabling interactions with diverse partners, including receptors, kinases, and cytoskeletal components. TRIP11 plays critical roles in maintaining Golgi structure, regulating protein sorting, and facilitating cell adhesion/migration. Dysregulation of TRIP11 is linked to cancers (e.g., prostate, breast), skeletal disorders (e.g., spondyloepiphyseal dysplasia), and thyroid hormone signaling defects.
TRIP11 antibodies are widely used in research to detect protein expression, localization, and interactions via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Polyclonal antibodies often target specific domains (e.g., C-terminal region), while monoclonal versions offer higher specificity. Validation typically includes knockout (KO) cell lines or siRNA knockdown to confirm signal loss. These antibodies help explore TRIP11's role in diseases, such as its oncogenic potential via EGFR trafficking or its involvement in skeletal development through dysregulated collagen secretion. Commercial TRIP11 antibodies vary in host species, clonality, and conjugates, requiring careful selection based on experimental needs.