Tubulin-specific chaperone cofactor C (TBCC) is a critical protein involved in the folding and assembly of β-tubulin, a key component of microtubules. It acts as a chaperone in the final step of the β-tubulin folding pathway, working alongside other cofactors (e.g., cofactors A, B, D, E) and the cytosolic chaperonin complex (CCT) to ensure proper tubulin heterodimer formation. TBCC’s role in maintaining microtubule integrity links it to essential cellular processes, including cell division, cytoskeletal organization, and intracellular transport.
Antibodies targeting TBCC are valuable tools for studying its expression, localization, and function. They are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to investigate TBCC’s interaction with tubulin and cofactors. Dysregulation of TBCC has been implicated in diseases such as cancer, where altered microtubule dynamics contribute to uncontrolled cell proliferation, and neurodevelopmental disorders, where TBCC mutations disrupt neuronal microtubule networks. Researchers also utilize TBCC antibodies to explore mechanisms of drug resistance in chemotherapy, as microtubule-targeting agents (e.g., taxanes) are common anticancer therapies. Both monoclonal and polyclonal anti-TBCC antibodies are available, often validated using knockout cell lines or siRNA-mediated knockdown to ensure specificity. These reagents continue to advance our understanding of tubulin biology and disease-associated TBCC anomalies.