TBCC Antibodies

Structure of TBCC

TBCC is a microtubule-binding protein with a molecular weight of approximately 55 kDa, and there are slight differences among different species:

The TBCC protein is composed of approximately 500 amino acids and its structure encompasses multiple functional domains, among which the core β -propeller structure is responsible for binding to tubulin. This protein affects cell division and morphological maintenance by regulating the depolymerization and recombination of microtubules. The key amino acids in its active center (such as conserved Glu residues) are crucial to microtubule kinetics. The tertiary structure of TBCC presents a typical spherical conformation, stabilizing the microtubule binding interface through charge interaction, while the C-terminal flexible region participates in the interaction with other cytoskeletal regulatory factors.

Fig. 1 Human TBCC protein family.¹

Key structural properties of TBCC:

• β -propeller domain
• Conserved acidic amino acid clusters
• Flexible C-end domain

Functions of TBCC

The main function of the protein encoded by the TBCC gene is to regulate microtubule dynamics and cell division, while also participating in a variety of cellular physiological processes:

The mechanism of action of TBCC protein is ATP-dependent, and its activity is strictly regulated by phosphorylation modifications (such as CDK1-mediated Ser89 phosphorylation). When forming a complex with the microtubule-binding protein TBCB, its depolymerization activity is significantly enhanced, indicating its core role in microtubule remodeling. The expression level of this protein increases in rapidly proliferating cells, suggesting its close association with the cell cycle process.

Applications of TBCC and TBCC Antibody in Literature

1. Guo, Yaru, et al. "TBCC Domain-Containing Protein Regulates Sporulation and Virulence of Phytophthora capsici via Nutrient-Responsive Signaling." International Journal of Molecular Sciences 25.22 (2024): 12301.https://doi.org/10.3390/ijms252212301

In this study, through transcriptomics and CRISPR-Cas9 technology, it was found that the pathogenic factor PcTBCC1 of Oomycetes (containing tubulin binding domain and chloroplast targeted peptide) was significantly upregulated in host interactions. After gene knockout, the formation, differentiation and pathogenicity of pathogenic bacteria spores were significantly weakened, and they were sensitive to osmotic stress, indicating that TBCC is a conserved pathogenic determinant and can be a potential target for ovulatory drugs.

2. Hage-Sleiman, Rouba, et al. "Tubulin binding cofactor C (TBCC) suppresses tumor growth and enhances chemosensitivity in human breast cancer cells." BMC cancer 10.1 (2010): 135.https://doi.org/10.1186/1471-2407-10-135

In this study, by regulating the expression of tubulin chaperone TBCC in breast cancer cells, it was found that overexpression of TBCC led to a reduction in polymerizable tubulin, a decrease in microtubule dynamics, and a delay in the G2/M phase of the cell cycle. In vivo experiments have shown that high expression of TBCC inhibits tumor growth and simultaneously enhances the sensitivity of cancer cells to microtubule drugs, suggesting that TBCC is a key factor in regulating tumor phenotypes and chemotherapy responses.

3. Garcia-Mayoral, Mª Flor, et al. "The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction." PloS one 6.10 (2011): e25912.https://doi.org/10.1371/journal.pone.0025912

Research has found that tubulin chaperone (TBCC) interacts with tubulin through its N-terminal disordered region and participates in spindle formation. The absence of TBCC leads to abnormal multipolar spindles and mitosis. NMR analysis revealed that the N-terminal of TBCC had a spectrin-like structure, and its 30-amino acid flexible fragment directly mediated tubulin recognition, providing new insights into the TBCC-Tubulin interaction mechanism.

4. Barrack, Keri L., et al. "Crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major." Molecular and Biochemical Parasitology 201.1 (2015): 26-30. https://doi.org/10.1016/j.molbiopara.2015.05.003

This study resolved the C-terminal domain of Leishmania TBCC protein (with A resolution of 2.2 A) and found that it presented a triangular prism structure formed by five right-handed β -helices. Structural comparison indicates that this β -helical surface may be involved in the interaction of the β-tubulin:GTP complex, revealing the molecular basis by which TBCC promotes GTPase activity.

5. Taheri, Aryan, et al. "Cryo-EM structures of the tubulin cofactors reveal the molecular basis for the biogenesis of alpha/beta-tubulin." bioRxiv (2024): 2024-01.https://doi.org/10.1101/2024.01.29.577855

In this study, the structure of the TBC-DEG-TBCC complex and αβ-tubulin was resolved by cryo-electron microscopy. It was found that TBCC pulled the C-terminal of α-tubulin by rotating the "lever arm" of TBCE clockwise, while TBCD fixed β-tubulin. The "vise" molecular mechanism of GTP hydrolysis-dependent tubulin assembly was revealed.

Creative Biolabs: TBCC Antibodies for Research

Creative Biolabs specializes in the production of high-quality TBCC antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom TBCC Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our TBCC antibodies, custom preparations, or technical support, contact us at email.