TBCA Antibodies

Background

The TBCA protein encoded by the TBCA gene, as a key component of the molecular chaperone complex, mainly participates in the correct folding of β-tubulin and the assembly process of tubulin heterodimers. This protein plays a significant role in maintaining genomic stability by maintaining the conformational stability of tubulin and ensuring the normal formation of the spindle during cell division. Research has found that mutations in the TBCA gene can disrupt the microtubule network structure, leading to abnormal neuronal development, which is closely related to the occurrence of various neurodegenerative diseases. As a core regulatory factor of the eukaryotic microtubule assembly system, its unique folding mechanism provides an important model for the study of protein conformational diseases. In recent years, the structure of the TBCA-tubulin complex resolved by cryo-electron microscopy technology has further deepened people's understanding of the folding pathway mediated by molecular chaperone.

Structure Function Application Advantage Our Products

Structure of TBCA

TBCA is a microtubulin folding chaperone with a molecular weight of approximately 12.8 kDa, and its precise molecular weight varies slightly among different eukaryotes.

Species	Human	Mouse	Yeast	Arabidopsis thaliana	Zebrafish
Molecular Weight (kDa)	12.8	12.7	13.2	12.9	12.6
Primary Structural Differences	Highly conservative β -folded core	90% homology to humans	The N-end extension area	Special acidic C-terminal	Retain all functional residues

This protein is composed of 109 amino acids and forms a typical α+β mixed folded conformation. The core of its three-dimensional structure consists of four anti-parallel β -folds, with three sets of α -helices distributed on both sides, jointly forming hydrophobic binding pockets. This pocket directly recognizes the intermediate domain of β -tubulin through phenylalanine at position 37 and leucine at position 73. It is particularly worth noting the acidic ring region formed at positions 85-92, where aspartic acid at position 87 and glutamic acid at position 91 stabilize the GTP binding site of tubulin through a hydrogen bond network, ensuring that β -tubulin can correctly complete the folding process.

Fig. 1 Comparison of the interacting face of TBCA, BAG1 and TBCC N-terminal domain.¹

Key structural properties of TBCA:

Typical α+β mixed fold conformation
The hydrophobic core is composed of four anti-parallel β -folds
Conserved acidic amino acid residues are involved in β -tubulin recognition
The C-terminal flexible region regulates tubulin dimer assembly

Functions of TBCA

The core function of the protein encoded by the TBCA gene is to mediate the folding and assembly of β -tubulin. Its main functional system includes:

Function	Description
Tubulin folding	As a molecular chaperone, it directly binds to the unfolded β -tubulin, preventing its aggregation and promoting the acquisition of the correct three-dimensional conformation.
Dimer assembly	The β -tubulin that assists in the folding process forms a functional heterodimer with α -tubulin.
Maintenance of microtubule networks	By regulating the supply quality of tubulin monomers, the normal dynamics of spindle microtubules during cell division can be guaranteed.
Stress protection	Stabilize the tubulin pool under conditions such as oxidative stress to prevent fibrotic aggregation caused by misfolding.
Neurodevelopmental support	In particular, it ensures a continuous supply of tubulin in neurons to support axon transport and synaptic plasticity.

This protein forms a specific recognition interface with the GTP binding domain of β -tubulin through its C-terminal acidic region. This interaction does not rely on ATP hydrolysis but achieves the folding catalysis of substrate proteins through conformational selection mechanisms, providing structurally correct functional units for microtubule assembly.

Applications of TBCA and TBCA Antibody in Literature

1. Nolasco, Sofia, et al. "Colchicine blocks tubulin heterodimer recycling by tubulin cofactors TBCA, TBCB, and TBCE." Frontiers in cell and developmental biology 9 (2021): 656273. https://doi.org/10.3389/fcell.2021.656273

Research has found that colicine, which is used to treat pericarditis, can inhibit the decomposition of tubulin dimer by TBCE/TBCB, leading to an increase in free TBCA. This, in turn, interferes with tubulin recovery by affecting the TBCA system, which may be its new anti-inflammatory mechanism.

2. Hillary, Robert F., et al. "Genome‐and epigenome‐wide studies of plasma protein biomarkers for Alzheimer's disease implicate TBCA and TREM2 in disease risk." Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring 14.1 (2022): e12280. https://doi.org/10.1002/dad2.12280

Research has found that the higher the levels of TBCA and TREM2 proteins in the blood, the lower the risk of Alzheimer's disease (AD). The research, through genomic methods, has revealed the genetic and epigenetic factors that regulate the levels of these AD-related proteins.

3. Danquah, Bright D., et al. "Mass Spectrometric analysis of antibody—Epitope peptide complex dissociation: Theoretical concept and practical procedure of binding strength characterization." Molecules 25.20 (2020): 4776. https://doi.org/10.1371/journal.pone.0042536

Research has found that the Tbca16 gene in mice negatively regulates the level of Tbca13 mRNA during testicular maturation through its sense and antisense transcripts. This post-transcriptional regulatory mechanism may play a key role in spermatogenesis that requires microtubule recombination.

4. Dai J, Gao J, Jiahui Gao, and Hongchao Dong. "Prognostic relevance and validation of ARPC1A in the progression of low-grade glioma." Aging (Albany NY) 16.14 (2024): 11162. https://doi.org/10.18632/aging.205952

Research has found that the set composed of mitochondrial-related genes such as TBCA is associated with the prognosis of low-grade glioma (LGG). Among them, the gene ARPC1A can promote the proliferation of LGG cells through the MAPK signaling pathway and is an important independent risk factor and potential biomarker.

5. Pickett, Sarah J., et al. "Interactions between nuclear and mitochondrial SNPs and Parkinson's disease risk." Mitochondrion 63 (2022): 85-88. https://doi.org/10.1016/j.mito.2022.02.002

Research has found that, unlike healthy individuals, patients with Parkinson's disease (PD) have specific combinations of nuclear genes such as TBCA and mitochondrial genes. The interaction of these combinations significantly affects the risk of developing Parkinson's disease.

Creative Biolabs: TBCA Antibodies for Research

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

Custom TBCA 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 TBCA antibodies, custom preparations, or technical support, contact us at email.

Reference

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