CTNNA1 Antibodies

Structure of CTNNA1

The molecular weight of the α-catenin encoded by the CTNNA1 gene is approximately 100 kDa. The value varies minimally among different species due to the conservation of functional domains, with only minor differences. The primary structure of this protein consists of approximately 906 amino acid residues, and its core is a 12-armed repeat domain structure. These domains fold in space and together form a rigid rod-like three-dimensional structure. Its secondary structure is mainly composed of α-helices, which are tightly stacked and give the protein mechanical stability. The N-terminal domain of the protein specifically binds to β-catenin, while the C-terminal region is responsible for connecting the actin cytoskeleton, thereby forming a crucial mechanical bridge within the cell membrane, stabilizing the adhesive connection between cells.

Fig. 1 UBE2O Triggers a CTNNA1 Binding Switch from β-Catenin to Vinculin via Ubiquitylation.¹

Key structural properties of CTNNA1:

• Made up of 12 series arm repetitive sequence of rigid rod structure
• N-terminal contains β-catenin binding domain, and C-terminal contains actin binding domain
• The mechanical stability of the protein scaffold is formed through the stacking of α-helices and β-sheets

Functions of CTNNA1

The main function of the CTNNA1 gene is to mediate and stabilize intercellular adhesion junctions. However, it is also widely involved in a variety of crucial cellular physiological processes, including mechanical signal transduction and gene expression regulation.

The function of α-catenin depends on its dynamic and competitive binding with multiple ligands (such as β-catenin and actin). This characteristic makes it a crucial hub that integrates extracellular adhesion signals with intracellular cytoskeletal activities, rather than a simple static connector.

Applications of CTNNA1 and CTNNA1 Antibody in Literature

1. Xiang, Dan, et al. "UBE2O-mediated ubiquitylation directs cytoplasmic CTNNA1 to promote cell-to-ECM adhesions." EMBO reports 26.22 (2025): 5431. https://doi.org/10.1038/s44319-025-00585-4

This study reveals that UBE2O selectively ubiquitinates cytoplasmic CTNNA1, regulating its interacting proteins to shift from β-catenin to vinculin, thereby promoting the maturation of adhesion plaques and the initial matrix adhesion during cell spreading. It elucidates a new mechanism of precise regulation of cell-ECM adhesion through ubiquitination as a molecular switch.

2. Guerra, Joana, et al. "Frequency of CDH1, CTNNA1 and CTNND1 germline variants in families with diffuse and mixed gastric cancer." Cancers 15.17 (2023): 4313. https://doi.org/https://doi.org/10.3390/cancers15174313

This study's analysis revealed that in patients with diffuse-type gastric cancer who met the HDGC criteria, the detection rate of germline pathogenic variants of CTNNA1 was 0.7%. However, in patients with mixed-type gastric cancer, no pathogenic variants of CDH1, CTNNA1, or CTNND1 were detected, suggesting that mixed-type gastric cancer may not need to be included in the relevant genetic testing criteria.

3. Tanner, Alexander, et al. "Clinical and genetic findings in CTNNA1-associated macular pattern dystrophy." Ophthalmology 128.6 (2021): 952-955. https://doi.org/10.1016/j.ophtha.2020.10.032

In this study, novel missense mutations in the CTNNA1 gene associated with butterfly-shaped pigmentary retinopathy were identified in six new families. The pathogenicity of these mutations was verified, and the phenotypic characteristics of the disease were further described through imaging.

4. Li, Mianyang, et al. "CTNNA1 hypermethylation, a frequent event in acute myeloid leukemia, is independently associated with an adverse outcome." Oncotarget 7.21 (2016): 31454. https://doi.org/10.18632/oncotarget.8962

This study found that the promoter of the CTNNA1 gene was highly methylated in acute myeloid leukemia. This was associated with unfavorable karyotypes and specific gene mutations, and it was an independent poor prognostic factor for the recurrence risk and prognosis of AML patients.

5. Pavel, Mariana, et al. "Cell type-specific YAP1-WWTR1/TAZ transcriptional responses after autophagy perturbations are determined by levels of α-catenins (CTNNA1 and CTNNA3)." Autophagy 17.7 (2021): 1788-1790. https://doi.org/10.1080/15548627.2021.1934273

This study reveals that α-catenin (CTNNA1) acts as a substrate for autophagy, and its level determines the directional impact of autophagy perturbation on the activity of the YAP1-WWTR1/TAZ signaling pathway. A mathematical model was constructed to clarify the timing and cell type specificity of this feedback regulation.

Creative Biolabs: CTNNA1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality CTNNA1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom CTNNA1 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 CTNNA1 antibodies, custom preparations, or technical support, contact us at email.