TCTN2 Antibody

What is TCTN2 and what is its cellular function?

TCTN2, also known as tectonic-2 or TECT2, is a type I membrane protein belonging to the tectonic family, which includes TCTN1, TCTN2, and TCTN3 . Functionally, TCTN2 serves as a component of the tectonic-like complex localized at the transition zone of primary cilia. This complex acts as a crucial barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes . Research in mouse models has demonstrated that tectonic proteins play essential roles in Hedgehog (Hh) signaling pathways and are necessary for proper ciliogenesis. The protein exists in multiple isoforms, with evidence of alternative splicing affecting its structure and potentially its function. Understanding TCTN2's cellular localization is critical for experimental design, as it primarily localizes to the intracellular side of the plasma membrane, which has implications for detection methodologies and functional studies.

What types of TCTN2 antibodies are available for research?

Researchers have access to both polyclonal and monoclonal antibodies against TCTN2, each with specific advantages for different experimental applications . Polyclonal antibodies, such as rabbit polyclonal antibodies, recognize multiple epitopes on the TCTN2 protein, potentially providing stronger signals in applications like Western blotting and immunohistochemistry. These antibodies have been validated for reactivity against human, mouse, and rat TCTN2 . Monoclonal antibodies offer higher specificity for particular epitopes and typically provide more consistent results across experiments. For instance, mouse monoclonal antibodies against TCTN2 have been developed for specific applications like Western blot, immunofluorescence, and flow cytometry . Various antibodies target different regions of TCTN2, including N-terminal, C-terminal, and internal regions, allowing researchers to select antibodies appropriate for their specific experimental questions. Some antibodies are available with conjugations such as biotin or fluorescent labels (e.g., AbBy Fluor® 750, AbBy Fluor® 680), facilitating direct detection in multiple experimental formats .

What is the molecular weight of TCTN2 and how does glycosylation affect its detection?

TCTN2 has a predicted molecular weight of approximately 77 kDa, but due to post-translational modifications, particularly glycosylation, it typically appears at a higher molecular weight in Western blot analyses . When detected by Western blot using either polyclonal or monoclonal antibodies, TCTN2 primarily appears as a band around 100 kDa in transfected cells and cancer cell lines . This higher-than-expected molecular weight is attributed to glycosylation at four potential glycosylation sites within the protein. Treatment of protein extracts with PNGase F, an enzyme that removes N-linked glycosylation, causes the immunoreactive band to shift to approximately 80 kDa, which more closely aligns with the predicted molecular weight of the unmodified protein . This glycosylation pattern provides important information for researchers, as variations in the glycosylation state may appear as multiple bands in Western blot analyses, and could potentially reflect functional differences in TCTN2 across different tissue types or disease states.

In which species can TCTN2 antibodies detect the target protein?

Most commercially available TCTN2 antibodies have been validated for reactivity against human, mouse, and rat TCTN2, making them valuable tools for comparative studies across these species . When selecting an antibody for cross-species studies, researchers should verify the specific reactivity profile of their chosen antibody, as epitope conservation may vary between species. Some antibodies may have broader cross-reactivity, while others may be optimized for a single species. For example, certain rabbit polyclonal antibodies have been confirmed to detect TCTN2 in human, mouse, and rat samples across multiple applications including ELISA, immunohistochemistry (IHC), immunofluorescence (IF), and immunoprecipitation (IP) . The species reactivity information is particularly important when designing experiments involving animal models or when working with conserved biological pathways across different organisms. Researchers should also be aware that antibody performance may vary between applications even within the same species, necessitating validation for each specific experimental context.

Which applications are TCTN2 antibodies suitable for?

TCTN2 antibodies have been validated for a diverse range of experimental applications, providing researchers with flexibility in their methodological approaches . For protein detection and quantification, Western blotting (WB) represents a primary application, allowing visualization of TCTN2's molecular weight and relative abundance. Immunohistochemistry (IHC) applications enable researchers to examine TCTN2 expression patterns in tissue sections, with both paraffin-embedded (IHC-P) and frozen (IHC-fro) tissue preparation methods supported by various antibodies . For cellular localization studies, immunofluorescence (IF) and immunocytochemistry (ICC) applications provide high-resolution visualization of TCTN2 distribution within cells, revealing its predominantly intracellular membrane localization . Additionally, immunoprecipitation (IP) allows isolation of TCTN2 and associated protein complexes for interaction studies, while ELISA techniques provide quantitative measurement capabilities . Some specialized antibodies have also been validated for flow cytometry (FACS), enabling analysis of TCTN2 expression in individual cells within heterogeneous populations .

What are the optimal dilutions for using TCTN2 antibodies in different applications?

Optimal antibody dilutions vary significantly based on the specific application, antibody format, and experimental conditions . For immunoprecipitation (IP) experiments, rabbit polyclonal TCTN2 antibodies typically perform well at dilutions ranging from 1:200 to 1:2000, allowing flexibility based on expression levels and antibody affinity . When performing immunohistochemistry (IHC), more concentrated antibody solutions are generally required, with recommended dilutions between 1:20 and 1:200 . Similarly, immunofluorescence (IF) applications typically require dilutions in the range of 1:20 to 1:200 to achieve optimal signal-to-noise ratios . These dilution ranges serve as starting points, and researchers should perform antibody titration experiments to determine the optimal concentration for their specific experimental conditions, sample types, and detection systems. Factors such as fixation method, antigen retrieval protocol, incubation time, and detection system can all influence the optimal antibody concentration. For quantitative applications like ELISA, careful calibration with standards and determination of linear range is essential for accurate results.

How should samples be prepared for optimal TCTN2 detection?

Sample preparation protocols significantly impact TCTN2 detection sensitivity and specificity across different applications . For Western blot analysis, complete cell lysis using detergent-based buffers with protease inhibitors is essential to solubilize membrane-associated TCTN2 while preserving its integrity. For immunofluorescence and immunocytochemistry applications, cell membrane permeabilization is critical, as TCTN2 localizes primarily to the intracellular side of the plasma membrane and is not accessible without permeabilization . Studies have demonstrated that TCTN2 is detectable at the plasma membrane level only in permeabilized cells treated with detergents like BRJ96, while remaining undetectable in non-permeabilized preparations . For immunohistochemistry applications using formalin-fixed paraffin-embedded (FFPE) tissues, antigen retrieval steps are typically necessary to unmask epitopes altered by fixation. When studying glycosylation states of TCTN2, researchers may consider treating samples with glycosidases like PNGase F to remove N-linked glycans, which shifts the apparent molecular weight from approximately 100 kDa to around 80 kDa .

What controls should be used when working with TCTN2 antibodies?

Implementing appropriate controls is essential for accurate interpretation of TCTN2 antibody-based experiments . Positive controls should include samples with verified TCTN2 expression, such as HCT15, HT29, HOP92, or OVCAR8 cell lines, which have been documented to express detectable levels of TCTN2 protein . Negative controls might include cell lines with low or undetectable TCTN2 expression, such as SKBR3, which shows very faint or negative bands in Western blot analyses . For genetic validation of antibody specificity, TCTN2 knockdown using siRNA represents an effective approach, with studies demonstrating significant reduction in both transcript and protein levels following siRNA treatment in multiple cell lines . Ideally, multiple siRNAs targeting different regions of TCTN2 should be used to confirm specificity, as demonstrated in HOP92, OVCAR8, and HCT15 cells . For immunostaining applications, secondary antibody-only controls are essential to rule out non-specific binding. When studying TCTN2 in tissues, appropriate normal tissue controls should be included alongside cancer samples to establish baseline expression levels and specificity of staining patterns.

What is the significance of TCTN2 expression in cancer tissues?

TCTN2 has emerged as a potentially significant tumor marker with oncogenic properties across multiple cancer types . Research has revealed TCTN2 expression in a significant percentage of colorectal cancer (CRC) samples (63.8%; P value <0.0001), as well as in lung (18%) and ovary (16%) cancer samples, while showing minimal or negative staining in corresponding normal tissues . This differential expression pattern suggests TCTN2 may play a role in oncogenesis or tumor progression. Functional studies further support TCTN2's oncogenic properties, as downregulation of TCTN2 in cancer cell lines resulted in reduced cell invasiveness and significantly decreased clonogenic growth in anchorage-independent conditions . For example, in the Boyden assay measuring cell migration and invasiveness, cells with reduced TCTN2 expression showed approximately a 3-fold reduction in invasive properties . Similarly, in soft agar assays assessing clonal growth, TCTN2 downregulation led to a marked decrease in clonogenic phenotype (up to 1 log reduction in colony numbers) . These findings collectively suggest that TCTN2 expression may contribute to aggressive cancer phenotypes, positioning it as both a potential diagnostic marker and therapeutic target.

What methods can be used to study TCTN2's role in cancer progression?

Researchers investigating TCTN2's role in cancer progression can employ multiple complementary approaches to generate comprehensive insights . Gene silencing techniques using siRNA or CRISPR-Cas9 systems provide powerful tools for functional studies, as demonstrated by experiments showing reduced invasiveness and clonogenic growth following TCTN2 downregulation . For studying protein expression patterns across cancer types and stages, immunohistochemistry on tissue microarrays (TMAs) enables high-throughput analysis of multiple patient samples simultaneously . Western blot analysis of cancer cell lines allows quantitative assessment of TCTN2 protein levels and glycosylation states, while qRT-PCR provides measurement of TCTN2 transcript levels to correlate with protein expression data . To investigate cellular localization and co-localization with other proteins, confocal microscopy with membrane permeabilization protocols has proven effective, revealing TCTN2's predominantly intracellular membrane localization . For functional assessments, invasion assays (such as Boyden chamber assays) and anchorage-independent growth assays (soft agar assays) provide valuable metrics of cancer cell aggressiveness that can be correlated with TCTN2 expression levels .

How can researchers interpret TCTN2 IHC scoring in clinical cancer samples?

Accurate interpretation of TCTN2 immunohistochemistry (IHC) results requires standardized scoring systems that account for both staining intensity and percentage of positive cells . Researchers have implemented a comprehensive IHC scoring system where the intensity of antibody staining (graded from 1 to 3) is multiplied by the percentage of positive cancer cells (from 1 to 100), yielding scores ranging from 1 to 300 . Using this methodology, samples are typically categorized as having strong or moderate staining when their IHC score exceeds 100 . In colorectal cancer studies, approximately 30% of samples showed strong or moderate staining (IHC score >100), compared to 10% in lung cancer and 0% in ovarian cancer, quantitatively confirming higher TCTN2 expression in colorectal cancers . When analyzing association with clinical parameters, it's important to categorize samples consistently, such as grouping them into "total positive" versus "medium-strong positive" categories as shown in comprehensive studies of colorectal cancer . Statistical analysis methods like Fisher's exact test can then be applied to determine significant associations between TCTN2 expression patterns and clinicopathological parameters, with P values less than 0.05 generally considered statistically significant .

How can researchers differentiate between different members of the tectonic family?

Distinguishing between the three tectonic family members (TCTN1, TCTN2, and TCTN3) requires careful selection of experimental approaches due to their structural similarities and potentially overlapping functions . Antibody-based methods necessitate selecting highly specific antibodies that target unique epitopes within each family member to avoid cross-reactivity. Researchers should perform extensive validation using overexpression and knockdown systems to confirm antibody specificity before conducting comparative studies. At the RNA level, quantitative PCR with carefully designed primers targeting unique regions of each transcript allows for specific amplification and quantification of individual tectonic family members. For functional differentiation, selective gene silencing using siRNA or CRISPR-Cas9 approaches targeting each family member individually enables assessment of their distinct roles in processes like Hedgehog signaling and ciliogenesis. When investigating protein complexes, immunoprecipitation combined with mass spectrometry can identify specific interaction partners for each tectonic family member, potentially revealing unique functional relationships. Researchers should also consider developmental timing and tissue-specific expression patterns, as different tectonic family members may have specialized roles in specific tissues or developmental stages.

What approaches can be used to study TCTN2's role in ciliogenesis?

Investigating TCTN2's involvement in ciliogenesis requires specialized techniques focusing on primary cilia structure and function . Immunofluorescence microscopy represents a cornerstone method, using antibodies against TCTN2 alongside cilia markers (such as acetylated tubulin) to examine co-localization patterns and potential changes during cilia formation. Studies have demonstrated that TCTN2 specifically marks the transition zone of primary cilia in human hTERT-RPE1 cells . For functional studies, TCTN2 gene silencing using siRNA or CRISPR-Cas9 allows researchers to assess the impact of TCTN2 deficiency on cilia formation, structure, and function. Time-lapse microscopy following TCTN2 knockdown can reveal dynamic aspects of ciliogenesis disruption. Transmission electron microscopy provides ultrastructural analysis of cilia in the presence or absence of TCTN2, potentially revealing specific structural defects. To investigate TCTN2's role in the tectonic-like complex at the cilia transition zone, proximity ligation assays or FRET (Fluorescence Resonance Energy Transfer) can be employed to examine protein-protein interactions in situ. Additionally, researchers can use pharmacological modulators of ciliogenesis to determine whether TCTN2 expression or localization changes in response to these interventions.

How does TCTN2 glycosylation impact its function and detection?

The glycosylation state of TCTN2 introduces important considerations for both functional studies and detection methodologies . Western blot analyses have revealed that TCTN2 typically appears at approximately 100 kDa, significantly higher than its predicted molecular weight of 77 kDa, due to the presence of N-linked glycans at four potential glycosylation sites . Treatment with PNGase F, which removes N-linked glycosylation, shifts the band to approximately 80 kDa, confirming glycosylation's contribution to the protein's apparent molecular weight . Researchers investigating glycosylation's functional impact should consider enzymatic deglycosylation experiments followed by functional assays to determine whether glycosylation affects TCTN2's localization, stability, or interaction with binding partners. Multiple immunoreactive bands observed in Western blots of cancer cell lines may represent different glycosylation states of TCTN2, potentially reflecting functional heterogeneity . For comprehensive glycosylation analysis, mass spectrometry approaches can identify specific glycosylation sites and glycan structures. Researchers should also consider whether glycosylation patterns vary across different tissues or disease states, potentially affecting antibody recognition and contributing to functional differences in TCTN2 biology.

What methodologies are recommended for studying TCTN2's potential as a cancer biomarker?

Evaluating TCTN2's utility as a cancer biomarker requires robust methodological approaches spanning discovery, validation, and clinical correlation . For biomarker discovery, screening tissue microarrays (TMAs) containing multiple cancer types alongside matched normal tissues using well-validated TCTN2 antibodies provides initial insights into expression patterns across diverse cancers . The discovery that TCTN2 shows significant expression in colorectal (63.8%), lung (18%), and ovary (16%) cancers while remaining largely negative in normal tissues exemplifies this approach . Following discovery, validation requires analyzing larger patient cohorts with comprehensive clinical data, as demonstrated in studies examining TCTN2 expression across 163 colorectal cancer cases with detailed clinicopathological information . Standardized scoring systems combining staining intensity and percentage of positive cells facilitate quantitative comparison across samples and cancer types . For clinical correlation, statistical analyses examining associations between TCTN2 expression and parameters like tumor stage, grade, and patient outcomes are essential. Receiver Operating Characteristic (ROC) curve analysis can assess TCTN2's diagnostic performance, determining optimal cutoff values for sensitivity and specificity . Multi-marker panels incorporating TCTN2 alongside other biomarkers may provide improved diagnostic or prognostic performance compared to single markers.

What are common issues when detecting TCTN2 by Western blot and how can they be resolved?

Western blot detection of TCTN2 presents several technical challenges requiring specific troubleshooting approaches . One common issue involves variations in apparent molecular weight, with TCTN2 typically appearing around 100 kDa due to glycosylation rather than at its predicted 77 kDa size . Researchers encountering unexpected band patterns should consider treating samples with glycosidases like PNGase F to remove N-linked glycans, which shifts the band to approximately 80 kDa and helps confirm band identity . Multiple immunoreactive bands may represent different glycosylation states rather than non-specific binding or degradation products . For membrane proteins like TCTN2, incomplete extraction can lead to weak signal, necessitating optimized lysis buffers containing appropriate detergents for membrane solubilization. When encountering weak or absent signals, researchers should verify TCTN2 expression in their cell line, as expression levels vary significantly across cell types (e.g., detectable in HCT15, HT29, and OVCAR8, but very faint in SKBR3) . For definitive confirmation of band specificity, TCTN2 knockdown using siRNA provides a powerful control, as demonstrated in studies showing significant reduction in the 100 kDa band following siRNA treatment .

How can researchers ensure specificity when using TCTN2 antibodies?

Ensuring antibody specificity is crucial for generating reliable data in TCTN2 research . Genetic validation approaches represent the gold standard, with siRNA-mediated knockdown providing compelling evidence of antibody specificity when the signal decreases proportionally to the reduction in TCTN2 expression . Studies have successfully validated antibody specificity using four different TCTN2-specific siRNAs (10 nM) to silence TCTN2 expression in cell lines like HOP92, OVCAR8, and HCT15, confirming reduction at both transcript (qRT-PCR) and protein (Western blot) levels . Overexpression systems provide complementary validation, as demonstrated by studies using HeLa cells transfected with full-length TCTN2, where both polyclonal and monoclonal antibodies specifically detected a main band around 100 kDa in TCTN2-transfected cells but not in control-transfected cells . For immunohistochemistry applications, comparing staining patterns between monoclonal and polyclonal antibodies targeting different TCTN2 epitopes helps confirm specificity, particularly when similar patterns are observed across antibodies . Additionally, peptide competition assays, where pre-incubation of the antibody with excess target peptide blocks specific binding, provide further validation of antibody specificity.

What considerations should be made when using TCTN2 antibodies for immunofluorescence studies?

Successful immunofluorescence detection of TCTN2 requires careful attention to several methodological aspects . Membrane permeabilization represents a critical step, as TCTN2 localizes primarily to the intracellular side of the plasma membrane and remains undetectable without permeabilization . Studies using confocal microscopy in cancer cell lines (HCT15, HOP92, HT29) have demonstrated that TCTN2 is detected at the plasma membrane level only after permeabilization with detergents like BRJ96 . Fixation methods significantly impact epitope preservation and accessibility, with paraformaldehyde fixation followed by detergent permeabilization commonly yielding good results for membrane proteins. When studying TCTN2 in ciliated cells, co-staining with established cilia markers (such as acetylated tubulin) helps establish TCTN2's specific localization to the ciliary transition zone . For quantitative studies, consistent imaging parameters and systematic analysis approaches are essential, ideally using automated image analysis software to minimize subjective interpretation. When performing co-localization studies with other proteins, appropriate controls for bleed-through between fluorescent channels are necessary. Finally, researchers should consider the target cell type's endogenous TCTN2 expression level, as detection sensitivity requirements will vary significantly between high-expressing cells (like HCT15 or HOP92) and those with lower expression.

How can researchers accurately quantify changes in TCTN2 expression levels?

Accurate quantification of TCTN2 expression changes requires rigorous methodological approaches at both protein and transcript levels . For protein-level quantification by Western blot, normalization to appropriate loading controls (such as GAPDH or β-actin) is essential, with densitometric analysis of band intensity providing relative quantification. When comparing expression across multiple samples or conditions, inclusion of a common reference sample on each blot allows normalization across experiments. For immunohistochemical quantification, standardized scoring systems combining staining intensity (graded 1-3) and percentage of positive cells (1-100) provide comprehensive assessment, as demonstrated in studies yielding scores ranging from 1 to 300 . For transcript-level quantification, quantitative real-time PCR (qRT-PCR) with carefully validated primers and appropriate reference genes enables precise measurement of TCTN2 mRNA levels. For example, studies validating siRNA efficiency have successfully used qRT-PCR to confirm TCTN2 transcript reduction . When correlating protein and transcript levels, researchers should consider potential post-transcriptional regulatory mechanisms. For functional studies examining TCTN2's impact on cellular phenotypes, dose-response relationships should be established by titrating siRNA concentrations or using inducible expression systems to create a range of TCTN2 expression levels.

What is the latest research on TCTN2's role in colorectal cancer?

Recent investigations have established TCTN2 as a significant marker in colorectal cancer with potential functional implications for cancer progression . Comprehensive immunohistochemical analysis of 163 colorectal cancer cases revealed remarkably high TCTN2 expression prevalence, with 95% of adenocarcinomas and 86% of mucinous subtypes showing positive staining . Detailed analysis across disease stages demonstrated ubiquitous TCTN2 positivity (100%) in Stage 1 CRC, with slightly decreasing frequencies in more advanced stages (91% in Stage 2, 98% in Stage 3, and 84% in Stage 4) . These expression patterns provide a foundation for exploring TCTN2 as a diagnostic marker for colorectal cancer. Functionally, TCTN2 appears to contribute to aggressive cancer phenotypes, as its downregulation in HT-29 colorectal cancer cells resulted in significantly reduced invasiveness (approximately 3-fold reduction) in Boyden chamber assays and markedly decreased clonogenic growth (up to 1 log reduction) in soft agar assays . These findings suggest that beyond its utility as a biomarker, TCTN2 may represent a potential therapeutic target in colorectal cancer. Future research directions include elucidating the molecular mechanisms through which TCTN2 promotes invasiveness and clonogenic growth, investigating its potential role in therapy resistance, and exploring its utility as part of multi-marker diagnostic or prognostic panels for colorectal cancer.

How does TCTN2 relate to primary cilia and Hedgehog signaling in cancer?

The relationship between TCTN2, primary cilia, and Hedgehog signaling represents an emerging area of cancer research with significant implications for understanding disease mechanisms . TCTN2 functions as a component of the tectonic-like complex at the primary cilium transition zone, where it acts as a barrier preventing diffusion of transmembrane proteins between the cilia and plasma membranes . This localization is particularly significant given that primary cilia serve as critical signaling centers in mammalian cells, including for the Hedgehog (Hh) pathway, which is frequently dysregulated in cancer. Studies in mice have established that tectonic family proteins, including TCTN2, play essential roles in Hedgehog signaling and ciliogenesis . The discovery of TCTN2 overexpression in multiple cancer types, particularly colorectal cancer (63.8%), raises important questions about whether aberrant TCTN2 expression contributes to cancer development or progression through alterations in ciliary function or Hedgehog pathway activity . Future research should investigate potential correlations between TCTN2 expression levels and Hedgehog pathway activation in cancer samples, examine whether TCTN2 knockdown affects Hedgehog target gene expression, and explore how TCTN2-mediated changes in cilia structure or function might impact cancer cell behavior, including proliferation, invasion, and response to therapy.

What methodological advances are improving TCTN2 research?

Recent methodological advances have significantly enhanced researchers' ability to study TCTN2 expression, localization, and function across diverse experimental contexts . In antibody technology, the development of highly specific monoclonal antibodies has improved detection consistency, while the availability of antibodies targeting different TCTN2 epitopes enables comprehensive protein characterization . The introduction of conjugated antibodies (with biotin or fluorescent labels like AbBy Fluor® 750 and AbBy Fluor® 680) has simplified detection workflows in applications like flow cytometry and immunofluorescence . In functional genomics, the application of precisely targeted gene silencing approaches using multiple siRNAs against TCTN2 has provided robust validation tools, as demonstrated in studies confirming antibody specificity in HOP92, OVCAR8, and HCT15 cells . Advanced imaging technologies, particularly confocal microscopy with membrane permeabilization protocols, have revealed TCTN2's specific localization to the intracellular side of the plasma membrane, information critical for appropriate experimental design . High-throughput screening approaches using tissue microarrays (TMAs) have accelerated biomarker discovery, enabling efficient evaluation of TCTN2 expression across multiple cancer types and clinicopathological parameters . Looking forward, emerging technologies like single-cell analysis, spatial transcriptomics, and advanced proteomics approaches promise to further refine our understanding of TCTN2's expression patterns and functional roles in development and disease.

What are the potential therapeutic implications of TCTN2 research?

The emerging understanding of TCTN2's role in cancer biology suggests several potential therapeutic applications warranting further investigation . First, TCTN2's differential expression between cancer and normal tissues, particularly in colorectal cancer where it shows high prevalence (95% in adenocarcinomas) while remaining largely negative in normal tissues, positions it as a potential diagnostic biomarker or therapeutic target with favorable selectivity profiles . Functional studies demonstrating reduced cancer cell invasiveness and clonogenic growth following TCTN2 downregulation provide proof-of-concept evidence that targeting TCTN2 could potentially attenuate aggressive cancer phenotypes . As a membrane protein, TCTN2 may be accessible to therapeutic antibodies or small molecules, though its predominantly intracellular orientation presents challenges requiring innovative delivery approaches . For diagnostic applications, the development of TCTN2-targeted imaging agents could potentially enhance cancer detection or monitoring. Given TCTN2's role in the tectonic-like complex at the primary cilium transition zone and its involvement in Hedgehog signaling, therapeutic strategies targeting TCTN2 might offer novel mechanisms to modulate these pathways, which are frequently dysregulated in cancer . Future translational research should evaluate whether TCTN2 expression levels correlate with treatment response to existing therapies, potentially providing predictive biomarkers to guide clinical decision-making.