znf367 Antibody

What is ZNF367 and why is it significant for research?

ZNF367 (Zinc Finger Protein 367) is a transcription factor containing a unique Cys2His2 zinc finger motif that functions as a central node in gene co-regulation networks. It is expressed primarily in embryonic or fetal erythroid tissue but is absent in most normal adult tissues . Its significance lies in its dual role as both a developmental regulator and a potential cancer biomarker. In neurodevelopment, ZNF367 acts as a key controller of neuroblast cell cycle, particularly in mitosis progression and spindle checkpoint regulation . Recent research has identified ZNF367 as overexpressed in several endocrine cancers, including adrenocortical carcinoma, malignant pheochromocytoma/paraganglioma, and thyroid cancer compared to normal tissues and benign tumors .

Research targeting ZNF367 is valuable because it represents a central hub in age-regulated gene networks, with implications for understanding both developmental processes and pathological conditions. ZNF367's tight regulation of cell cycle processes makes it a compelling target for investigating fundamental cellular mechanisms .

What are the primary applications for ZNF367 antibodies in research?

ZNF367 antibodies serve multiple research applications across developmental biology, cancer research, and aging studies. The primary applications include:

When selecting ZNF367 antibodies, researchers should consider species reactivity, which can include human, mouse, rat, and even Xenopus laevis and zebrafish for comparative studies . The choice of application determines the appropriate antibody format and validation requirements. For instance, Western blotting typically requires antibodies validated for denatured proteins, while IHC applications need antibodies that recognize the native protein in fixed tissue contexts .

How should I validate the specificity of ZNF367 antibodies?

Validating antibody specificity is crucial for generating reliable research data. For ZNF367 antibodies, a multi-step validation approach is recommended:

• Positive and negative controls: Use tissues or cell lines with known ZNF367 expression patterns. Based on existing research, breast cancer cell lines (MDA-MB-231, SKBR3), adrenocortical carcinoma lines (SW13), and thyroid cancer cells (TPC-1) express ZNF367 and can serve as positive controls . Normal adult tissues generally show low expression and can serve as negative controls.

• Knockdown/knockout verification: Utilize siRNA or CRISPR techniques to reduce or eliminate ZNF367 expression. Previous studies have achieved up to 80% knockdown of ZNF367 mRNA and protein expression using siRNA approaches . This creates an excellent negative control to confirm antibody specificity.

• Cross-reactivity assessment: Test the antibody against related zinc finger proteins to ensure it doesn't cross-react with other family members.

• Western blot analysis: Verify that the antibody detects a protein of the expected molecular weight (~42-45 kDa for human ZNF367).

• Peptide competition: Pre-incubate the antibody with a blocking peptide corresponding to the immunogen to confirm signal specificity.

Remember that validation should be performed in the specific experimental context and biological system you are studying, as antibody performance can vary across different applications and tissues .

What experimental conditions are optimal for detecting ZNF367 in Western blotting?

For optimal Western blot detection of ZNF367, consider the following methodological recommendations:

• Protein extraction: Use RIPA lysis buffer for total protein extraction as demonstrated in previous ZNF367 studies . This provides good solubilization of membrane and nuclear proteins.

• Gel concentration: A 7.5% SDS-PAGE gel is recommended based on successful detection in previous studies . This concentration provides good separation of proteins in the 40-50 kDa range where ZNF367 is expected.

• Blocking conditions: Block membranes with 5% nonfat milk in TBST for 1-2 hours at room temperature to minimize background .

• Antibody incubation: Incubate with primary ZNF367 antibody overnight at 4°C followed by appropriate secondary antibody incubation for 2 hours at room temperature .

• Loading control: β-tubulin has been successfully used as a loading control in ZNF367 Western blots .

• Detection system: Use an ECL detection system for visualization of protein bands .

• Sample types: ZNF367 has been successfully detected in various cell lines including MDA-MB-231, SKBR3, SW13, and TPC-1 .

Troubleshooting tip: If you encounter weak signals, consider increasing protein concentration, extending primary antibody incubation time, or using a more sensitive detection system such as enhanced chemiluminescence plus (ECL+) or fluorescent secondary antibodies.

How can I investigate ZNF367's role in cell cycle regulation using antibody-based approaches?

ZNF367 functions as a key controller of the neuroblast cell cycle, particularly in mitosis progression and spindle checkpoint regulation . To investigate this role using antibody-based approaches:

• Co-immunoprecipitation (Co-IP): Use anti-ZNF367 antibodies to pull down ZNF367 and identify interacting partners involved in cell cycle regulation. Previous research indicates potential interactions with proteins involved in mitotic spindle checkpoint, making FANCD2, SKA3, and SMC2 promising candidates for investigation .

• Chromatin immunoprecipitation (ChIP): Employ ZNF367 antibodies to identify genomic binding sites. This approach can reveal direct transcriptional targets of ZNF367 related to cell cycle control. Research has shown that ZNF367 may regulate genes like FANCD2, SKA3, and SMC2, which are involved in mitosis progression and spindle checkpoint .

• Immunofluorescence microscopy: Combine ZNF367 antibodies with markers of cell cycle phases (such as phospho-H3 for mitosis) to visualize ZNF367 localization during different stages of the cell cycle. Previous research has shown increased phospho-H3 staining in ZNF367 morphants, suggesting a role in mitotic regulation .

• Proximity ligation assay (PLA): Use this technique to detect and visualize protein-protein interactions between ZNF367 and suspected cell cycle regulators within cells.

• Flow cytometry: Combine ZNF367 antibody staining with DNA content analysis to correlate ZNF367 expression levels with specific cell cycle phases. Research indicates ZNF367 may be particularly important in M phase, as evidenced by increased Cyclin B1 expression in ZNF367 morphants .

For experimental design, consider that ZNF367 morphants showed increased expression of pcna and cyclin B1, suggesting ZNF367 may regulate G2/M transition or mitotic progression . When interpreting results, remember that ZNF367 appears to function in the maintenance of neuroblast populations and cell cycle exit rather than initial neuronal specification .

What methodological approaches can I use to study ZNF367's involvement in cancer progression?

ZNF367 has been implicated in cancer progression, with studies showing it is overexpressed in adrenocortical carcinoma, malignant pheochromocytoma/paraganglioma, and thyroid cancer . For investigating its role in oncogenesis:

Methodological consideration: For relevant cancer models, consider using SW13 and BD140A (adrenocortical carcinoma), TPC-1 (papillary thyroid cancer), and MDA-MB-231 and SKBR3 (breast cancer) cell lines, which have been successfully used in ZNF367 research .

How can I explore the relationship between ZNF367 and microRNA regulation?

ZNF367 expression has been shown to be regulated by microRNAs, particularly miR-195 . To investigate this regulatory relationship:

• Luciferase reporter assays: Design reporter constructs containing the ZNF367 3'UTR with wild-type and mutated miRNA binding sites. This approach has been used to demonstrate that miR-195 directly regulates ZNF367 expression . The methodology involves:

  • Amplifying the ZNF367 3'UTR region and subcloning it into a luciferase reporter vector

  • Creating mutant versions with altered miRNA binding sites

  • Co-transfecting cells with the reporter constructs and miRNA mimics/inhibitors

  • Measuring luciferase activity to assess direct regulation

• miRNA-mRNA correlation analysis: Analyze expression databases to identify inverse correlations between ZNF367 and candidate miRNAs. Integrated gene and microRNA expression analyses have previously shown an inverse correlation between ZNF367 and miR-195 expression .

• miRNA overexpression/inhibition: Manipulate miRNA levels and assess effects on ZNF367 expression using ZNF367 antibodies in Western blot or IHC applications.

• RNA immunoprecipitation (RIP): Use antibodies against miRNA processing components (e.g., Ago2) to immunoprecipitate miRNA-mRNA complexes and assess ZNF367 mRNA enrichment.

• Bioinformatic prediction: Utilize tools like TargetScan, miRanda, or PicTar to identify potential miRNA binding sites in the ZNF367 3'UTR. Validate these predictions experimentally using the methods above.

For comprehensive analysis, investigate both direct miRNA targeting of ZNF367 and indirect effects through regulatory networks. Consider that miR-195 regulation of ZNF367 has been shown to influence cancer cell invasion, suggesting functional significance of this regulatory axis .

What experimental design is appropriate for investigating ZNF367's role in neurogenesis?

ZNF367 has been identified as an important factor in neurogenesis, particularly during embryonic development . To investigate its role in this process:

• Knockdown studies in model organisms: Use morpholino oligonucleotides or CRISPR/Cas9 to reduce ZNF367 expression in neurogenesis models. Previous research in Xenopus used specific antisense oligonucleotide morpholinos to block translation of endogenous ZNF367 mRNA, targeting neural tissue through unilateral injection into one dorso-animal blastomere at the four-cell stage .

• Neural marker analysis: Assess the effects of ZNF367 manipulation on neuronal markers. Previous work demonstrated that ZNF367 morphants showed strong reduction of post-mitotic neuronal markers (N-tubulin, elrC/HuC) but no effect on the proneural marker ngnr1, suggesting ZNF367 functions in neuronal differentiation rather than specification .

• Neural progenitor assessment: Evaluate changes in neural progenitor populations using stemness markers. Research has shown that ZNF367 morphants display expanded expression domains of stemness genes (sox2, rx1), indicating a larger population of progenitors and suggesting that ZNF367 knockdown enhances self-renewal of progenitors at the expense of differentiation .

• Cell cycle analysis in neural contexts: Examine proliferation markers and mitotic indices. Previous studies utilized pcna expression analysis and phospho-H3 antibody staining to demonstrate increased mitotic activity in ZNF367 morphants .

• Rescue experiments: Perform functional rescue through co-injection of ZNF367 mRNA to confirm specificity of observed phenotypes. This approach successfully restored normal expression of sox2 and elrC markers in 25-30% of ZNF367 morphants .

Methodological consideration: For gene expression analysis, both whole-mount in situ hybridization (WISH) and qRT-PCR have been successfully employed to assess changes in neuronal markers (N-tubulin, elrC), stemness genes (sox2, rx1), and cell cycle regulators (pcna, cyclin B1) following ZNF367 manipulation .

How can I investigate potential ZNF367 transcriptional targets using chromatin immunoprecipitation?

To identify direct transcriptional targets of ZNF367, Chromatin Immunoprecipitation (ChIP) is a powerful approach. Based on existing research on ZNF367's role in cell cycle regulation and cancer:

• ChIP-Seq experimental design:

  • Crosslinking: Treat cells expressing ZNF367 with formaldehyde (typically 1% for 10 minutes) to crosslink protein-DNA complexes.

  • Chromatin fragmentation: Sonicate chromatin to generate fragments of 200-500 bp.

  • Immunoprecipitation: Use validated ZNF367 antibodies to pull down ZNF367-bound DNA fragments.

  • Sequencing and analysis: Sequence immunoprecipitated DNA and analyze enrichment patterns to identify binding sites.

• Target validation using ChIP-qPCR:

  • Based on existing research, prioritize genes involved in mitosis and spindle checkpoint for validation, including FANCD2, SKA3, and SMC2, which showed altered expression in ZNF367 morphants .

  • Design primers targeting promoter regions of these genes for qPCR analysis of ChIP samples.

• Integration with transcriptome data:

  • Combine ChIP-Seq data with RNA-Seq data from ZNF367 knockdown or overexpression experiments to distinguish direct transcriptional targets from indirect effects.

  • Previous research using weighted-gene co-expression network analysis identified FANCD2 and SKA3 as possible targets of ZNF367 .

• Motif analysis and binding site characterization:

  • Analyze ZNF367 binding sites to identify consensus DNA-binding motifs.

  • Consider that ZNF367 contains a Cys2His2 zinc finger motif, which typically recognizes specific DNA sequences .

• Functional validation of binding sites:

  • Use luciferase reporter assays with wild-type and mutated binding sites to confirm functional significance of ZNF367 binding.

  • This approach has been successfully used to study transcriptional regulation by ZNF367 of KIF15 in breast cancer cells .

For cancer research applications, consider focusing on cell cycle-related genes, as weighted-gene co-expression network analysis revealed that ZNF367-containing modules are enriched in genes involved in cell cycle progression, particularly those related to mitosis and spindle checkpoint .

What are the optimal fixation and antigen retrieval methods for ZNF367 immunohistochemistry?

Successful immunohistochemical detection of ZNF367 requires optimization of fixation and antigen retrieval protocols. Based on research practices with nuclear transcription factors and zinc finger proteins:

• Fixation protocols:

  • FFPE tissues: 10% neutral buffered formalin fixation for 24-48 hours is standard.

  • Frozen sections: 4% paraformaldehyde fixation for 15-20 minutes provides good preservation of antigenicity.

  • Cell preparations: 4% paraformaldehyde for 10-15 minutes at room temperature.

• Antigen retrieval methods:

  • Heat-induced epitope retrieval (HIER): Use citrate buffer (pH 6.0) or EDTA buffer (pH 9.0) with heating to 95-100°C for 20 minutes.

  • For zinc finger proteins like ZNF367: EDTA buffer (pH 9.0) often provides superior results by better exposing the zinc finger domains.

• Blocking conditions:

  • Use 5-10% normal serum (from the species in which the secondary antibody was raised) with 1% BSA in PBS.

  • Include 0.1-0.3% Triton X-100 for nuclear antigens like ZNF367 to improve antibody penetration.

• Signal amplification:

  • Consider tyramide signal amplification (TSA) for detecting low-abundance transcription factors.

  • Polymer-based detection systems often provide better sensitivity than avidin-biotin methods for nuclear antigens.

• Controls and validation:

  • Use positive control tissues known to express ZNF367 (e.g., embryonic tissue, cancer samples from adrenocortical carcinoma, thyroid cancer) .

  • Include antibody validation controls such as peptide competition or tissues from knockdown models.

For cancer tissue analysis, note that ZNF367 shows differential expression between normal and malignant tissues in several endocrine cancers, making careful optimization and inclusion of appropriate controls essential for accurate interpretation .

How can I troubleshoot non-specific binding issues with ZNF367 antibodies?

Non-specific binding is a common challenge when working with antibodies against transcription factors like ZNF367. Here are methodological approaches to troubleshoot and minimize these issues:

• Western blot non-specificity:

  • Increase stringency: Use TBST with higher Tween-20 concentration (0.1-0.3%) for washing.

  • Optimize blocking: Try alternative blocking agents such as 5% BSA or commercial blockers if milk proteins cause background.

  • Titrate antibody: Perform a dilution series to find the optimal concentration that maximizes specific signal while minimizing background.

  • Pre-adsorption: Incubate antibody with cell/tissue lysate from ZNF367-negative samples before use.

• Immunohistochemistry background:

  • Endogenous peroxidase quenching: Ensure complete blocking with 0.3-3% H₂O₂ for 10-30 minutes.

  • Endogenous biotin blocking: If using biotin-based detection, block endogenous biotin with avidin/biotin blocking kit.

  • Increase washing: Extend washing steps between antibody incubations.

  • Reduce antibody concentration: Try more dilute antibody solutions with longer incubation times.

• Cross-reactivity assessment:

  • Peptide competition: Pre-incubate antibody with immunizing peptide to confirm signal specificity.

  • Knockout/knockdown validation: Compare staining patterns in samples with normal versus reduced ZNF367 expression.

  • Multiple antibodies: If possible, use antibodies targeting different epitopes of ZNF367 to confirm staining patterns.

• Sample-specific considerations:

  • Tissue autofluorescence: For immunofluorescence applications, treat sections with Sudan Black B (0.1% in 70% ethanol) to reduce autofluorescence.

  • Biotin-rich tissues: Use biotin-free detection systems for tissues with high endogenous biotin (e.g., liver, kidney).

Based on the research literature, ZNF367 antibodies have been successfully applied in Western blotting, ELISA, and IHC applications , but careful optimization is necessary for each specific experimental context.

What approaches can I use to quantify ZNF367 expression levels in complex tissue samples?

Accurate quantification of ZNF367 expression in heterogeneous tissue samples requires carefully selected methodological approaches:

• Immunohistochemistry with digital image analysis:

  • Use ZNF367 antibodies validated for IHC applications .

  • Employ whole slide scanning and digital image analysis software to quantify:

    • Percentage of positive cells

    • Staining intensity (using H-score or Allred scoring systems)

    • Nuclear versus cytoplasmic localization

  • This approach has been used to analyze ZNF367 expression in cancer tissues from the Human Protein Atlas .

• Multiplex immunofluorescence:

  • Combine ZNF367 antibody with markers for specific cell types to quantify expression in distinct cell populations.

  • Use spectral imaging systems to separate fluorophores and reduce autofluorescence.

  • Analyze co-localization with cell-specific markers to determine expression patterns in different cell types.

• Tissue microdissection with protein quantification:

  • Use laser capture microdissection to isolate specific regions or cell types.

  • Extract proteins and perform Western blot analysis with ZNF367 antibodies.

  • Quantify band intensity relative to loading controls (β-tubulin has been successfully used) .

• Single-cell analysis approaches:

  • Mass cytometry (CyTOF): Label ZNF367 antibody with metal isotopes for high-dimensional analysis at single-cell resolution.

  • Flow cytometry: Perform intracellular staining for ZNF367 combined with surface markers for cell identification.

• Quantitative image analysis metrics:

  Measurement	Application	Advantages
  H-score (0-300)	IHC quantification	Combines intensity and percentage of positive cells
  Mean fluorescence intensity	Immunofluorescence	Provides continuous variable for statistical analysis
  Nuclear/cytoplasmic ratio	Subcellular localization	Assesses functional status of transcription factors
  Colocalization coefficients	Multi-marker studies	Quantifies association with other proteins

When interpreting ZNF367 expression data, consider that it shows differential expression patterns between normal tissues and cancer samples, with overexpression observed in several endocrine cancer types . For normal tissues, expression is primarily limited to embryonic or fetal erythroid tissue with absence in most normal adult tissues .

How can I investigate the ZNF367-KIF15 axis in cancer progression?

Recent research has identified a functional relationship between ZNF367 and KIF15 in cancer progression, particularly in breast cancer . To investigate this axis:

When designing experiments, consider that ZNF367-induced transcriptional activation of KIF15 has been implicated in accelerating the progression of breast cancer . This provides a conceptual framework for investigating similar regulatory relationships in other cancer types where ZNF367 is overexpressed, such as adrenocortical carcinoma, pheochromocytoma/paraganglioma, and thyroid cancer .

What approaches can help me understand ZNF367's role in the miR-195-ZNF367-ITGA3 regulatory axis?

Research has identified a regulatory axis involving miR-195, ZNF367, and ITGA3 (integrin alpha 3) that influences cancer progression . To investigate this pathway:

• miRNA-target validation:

  • Luciferase reporter assays: Construct reporters containing the ZNF367 3'UTR with wild-type or mutated miR-195 binding sites to confirm direct regulation .

  • Site-directed mutagenesis: Introduce specific mutations in predicted miR-195 binding sites to identify the critical regulatory elements.

  • miRNA mimic/inhibitor studies: Transfect cells with miR-195 mimics or inhibitors and assess effects on ZNF367 expression using antibody-based detection methods.

• ZNF367-ITGA3 regulatory relationship:

  • ChIP analysis: Use ZNF367 antibodies to determine if ZNF367 directly binds to the ITGA3 promoter.

  • Expression correlation: Perform Western blot and qRT-PCR analyses to assess how ZNF367 manipulation affects ITGA3 expression levels .

  • Promoter analysis: Create ITGA3 promoter reporter constructs to test direct transcriptional regulation by ZNF367.

• Functional significance assessment:

  • Cell invasion assays: Manipulate components of the miR-195-ZNF367-ITGA3 axis individually and in combination to determine effects on cancer cell invasion .

  • Adhesion assays: Measure cell adhesion to extracellular matrix proteins following manipulation of pathway components.

  • In vivo studies: Develop xenograft models with altered expression of pathway components to assess effects on tumor growth and metastasis.

• Pathway integration analysis:

  • Gene Ontology (GO) and KEGG pathway analysis: Identify broader pathways affected by this regulatory axis using bioinformatics approaches .

  • Protein interaction network analysis: Identify additional proteins that interact with components of this axis using proteomic approaches.

When interpreting results, consider that this regulatory axis has been shown to inhibit cancer progression, with miR-195 directly targeting ZNF367, and ZNF367 in turn regulating ITGA3 expression . This provides a mechanistic framework for understanding how alterations in ZNF367 expression influence cancer cell behavior through downstream effects on integrin-mediated adhesion and signaling.

How can I study age-related changes in ZNF367 expression and function?

ZNF367 has been identified as an age-regulated gene that represents a central node in gene co-regulation networks during aging . To investigate age-related aspects of ZNF367:

• Age-dependent expression analysis:

  • Cross-sectional tissue sampling: Collect tissue samples from different age groups and assess ZNF367 expression using antibody-based methods (Western blot, IHC) and qRT-PCR.

  • Longitudinal studies in model organisms: Monitor ZNF367 expression over time in accessible tissues from model organisms.

  • Single-cell transcriptomics: Analyze age-related changes in ZNF367 expression at the single-cell level to identify cell type-specific alterations.

• Neural stem cell aging models:

  • In vitro aging systems: Establish neural stem cell cultures and analyze ZNF367 expression and function across multiple passages as a model of cellular aging.

  • Neurosphere assays: Compare neurosphere formation capacity in relation to ZNF367 expression levels in young versus aged neural stem cells.

  • Age-related niche effects: Co-culture neural stem cells with young or aged niche cells and assess effects on ZNF367 expression and function.

• Next-generation sequencing approaches:

  • RNA-Seq across age groups: Perform differential expression analysis to identify age-regulated genes co-expressed with ZNF367 .

  • ChIP-Seq across age groups: Analyze age-dependent changes in ZNF367 binding patterns to identify alterations in its regulatory targets.

  • ATAC-Seq: Assess changes in chromatin accessibility at ZNF367 binding sites during aging.

• Co-expression network analysis:

  • Weighted gene co-expression network analysis (WGCNA): Identify modules of co-expressed genes containing ZNF367 across different ages .

  • Hub gene identification: Assess whether ZNF367 maintains its position as a hub gene across different age groups (previously identified in the 98th percentile of connectivity in N. furzeri and 92nd percentile in human cells) .

When designing age-related studies, consider that ZNF367's role during embryonic neurogenesis correlates with its age-related decline, suggesting potential implications for adult neurogenesis and maintenance of neural function . This provides a conceptual framework for investigating whether age-related declines in ZNF367 contribute to reduced neural stem cell functionality and increased neurodegenerative disease risk with age.

What emerging technologies might enhance ZNF367 antibody-based research?

As research on ZNF367 continues to evolve, several emerging technologies offer promising opportunities to advance antibody-based investigations:

• Proximity-dependent biotinylation (BioID/TurboID):

  • Fuse ZNF367 to a biotin ligase to identify proximal proteins in living cells.

  • This approach could reveal previously unknown interaction partners of ZNF367 in different cellular contexts.

  • Subsequent pull-down of biotinylated proteins followed by mass spectrometry can map the local protein interaction network.

• Super-resolution microscopy:

  • Apply techniques like STORM, PALM, or STED microscopy with ZNF367 antibodies to visualize subnuclear localization at nanometer resolution.

  • This could reveal precise spatial relationships between ZNF367 and chromatin or other nuclear components.

  • Multicolor super-resolution imaging could map ZNF367's relationship to transcriptional complexes and nuclear architecture.

• CRISPR-based technologies:

  • CUT&RUN/CUT&TAG: Combine ZNF367 antibodies with targeted nuclease activity for more sensitive and specific chromatin profiling than traditional ChIP.

  • CRISPR activation/repression: Target ZNF367 regulatory elements to modulate expression with greater precision than traditional overexpression/knockdown approaches.

  • CRISPR base editing: Introduce specific mutations in ZNF367 binding sites to dissect functional domains.

• Spatial transcriptomics/proteomics:

  • Combine ZNF367 antibody staining with spatial transcriptomics to correlate its expression/localization with gene expression patterns across tissue sections.

  • This approach would be particularly valuable for studying ZNF367's role in developmental contexts or heterogeneous tumors.

• Single-cell antibody-based technologies:

  • CITE-seq/REAP-seq: Combine antibody detection with single-cell RNA-seq to correlate ZNF367 protein levels with transcriptional states.

  • Single-cell CyTOF: Use metal-labeled ZNF367 antibodies for high-dimensional analysis of protein expression at single-cell resolution.

These emerging technologies could address current knowledge gaps, such as the precise mechanisms by which ZNF367 regulates cell cycle progression, its role in adult neurogenesis, and how its dysregulation contributes to cancer development and progression.

What are the most promising therapeutic applications targeting the ZNF367 pathway?

Based on current understanding of ZNF367's functions in development and disease, several therapeutic approaches show promise:

• microRNA-based therapies:

  • miR-195 mimics: Since miR-195 has been shown to directly regulate ZNF367 expression , developing miR-195 mimics could help normalize ZNF367 levels in cancers where it is overexpressed.

  • Target delivery systems: Develop nanoparticle-based or exosome-based delivery systems to target miR-195 mimics specifically to cancer cells.

  • Combinatorial approaches: Combine miR-195-based therapies with conventional treatments to enhance efficacy.

• Small molecule inhibitors:

  • Zinc finger domain targeting: Design small molecules that interfere with ZNF367 DNA binding capability.

  • Protein-protein interaction disruptors: Develop compounds that disrupt critical interactions between ZNF367 and its cofactors based on protein interaction mapping.

  • Degrader technologies: Apply targeted protein degradation approaches (e.g., PROTACs) to selectively eliminate ZNF367 protein.

• Gene therapy approaches:

  • CRISPR-based gene editing: Correct aberrant ZNF367 expression in cancer cells or introduce functional ZNF367 in neurological conditions where its function is impaired.

  • Viral vector delivery: Develop vectors for tissue-specific modulation of ZNF367 expression.

  • Regulatable expression systems: Create systems for controlled expression of ZNF367 to maintain appropriate levels.

• Targeting downstream effectors:

  • KIF15 inhibition: In contexts where the ZNF367-KIF15 axis promotes cancer progression , develop specific inhibitors of KIF15.

  • ITGA3 modulation: Target integrin signaling in cancers where the miR-195-ZNF367-ITGA3 axis is dysregulated .

• Neural regeneration applications:

  • Stem cell therapies: Modulate ZNF367 expression in neural stem cells to enhance their regenerative capacity.

  • Neuroprotective strategies: Develop approaches to maintain appropriate ZNF367 levels during aging to support neural stem cell functionality.

When considering therapeutic development, it's important to note that ZNF367's roles may be context-dependent, as it can inhibit cancer progression in some contexts while promoting it in others . Therefore, careful assessment of its function in specific disease contexts is essential for successful therapeutic targeting.