TRIM55 Antibody

What is TRIM55 and why is it important in biomedical research?

TRIM55 (Tripartite Motif Containing 55), also known as muscle-specific ring finger 2 (Murf2), is an E3 ubiquitin ligase belonging to the TRIM protein family. It plays crucial roles in protein degradation and immune response regulation . TRIM55 has emerged as a significant research target due to its involvement in various diseases, including multiple cancer types and autoimmune disorders. Its functional importance stems from its ability to regulate protein degradation through the ubiquitin-proteasome pathway, affecting critical cellular processes related to cancer development, immune response, and cellular signaling .

What are the common applications of TRIM55 antibodies in research?

TRIM55 antibodies are primarily utilized in these research applications:

• Western blot analysis (WB): Used for detecting and quantifying TRIM55 protein expression in tissue samples and cell lines, typically at dilutions ranging from 1:500 to 1:2000 .

• Immunohistochemistry (IHC): Applied to examine TRIM55 expression patterns in tissue sections, particularly in cancer tissues versus adjacent normal tissues .

• Co-immunoprecipitation (Co-IP): Employed to investigate protein-protein interactions between TRIM55 and its binding partners, such as c-Myc, NF90, and p100 .

• Immunofluorescence: Used to visualize the subcellular localization of TRIM55 and its interactions with other proteins .

What tissue types and cell lines are typically used for TRIM55 research?

Research on TRIM55 commonly utilizes:

• Cancer cell lines: HGC27 and SGC7901 (gastric cancer) , LO2 and HepG2 (liver cancer) , colorectal cancer cell lines

• Tissue samples: Colorectal cancer tissues, hepatocellular carcinoma tissues, gastric cancer tissues, and corresponding adjacent normal tissues

• Murine models: For in vivo studies of cancer development and immune responses

• Skeletal muscle: As TRIM55 was originally identified as a muscle-specific protein (hence its alternative name Murf2)

What are the key considerations for optimizing TRIM55 antibody use in Western blot?

When optimizing TRIM55 antibody for Western blot, researchers should consider:

• Antibody concentration: Recommended dilutions typically range from 1:500 to 1:2000, depending on the specific antibody and sample type .

• Sample preparation: Proper lysis buffers containing protease inhibitors are essential to prevent TRIM55 degradation during protein extraction.

• Positive controls: Include known TRIM55-expressing samples such as LO2, HepG2, or mouse skeletal muscle as positive controls .

• Storage conditions: Store the antibody at -20°C and avoid freeze-thaw cycles to maintain reactivity. Typically stored in PBS with 0.02% sodium azide and 50% glycerol at pH 7.3 .

• Blocking conditions: Optimize blocking solutions to minimize background while maintaining specific TRIM55 signal.

How can researchers resolve contradictory findings regarding TRIM55's role in hepatocellular carcinoma?

The literature contains seemingly contradictory findings regarding TRIM55's role in hepatocellular carcinoma (HCC), with some studies suggesting it suppresses HCC progression while others indicate it promotes proliferation . To address these contradictions, researchers should:

• Perform comprehensive expression analysis across diverse HCC patient cohorts, considering:

  • Clinical characteristics (tumor size, AFP levels, etiology)

  • Disease stage and differentiation status

  • Genetic background variations

• Design mechanistic studies to examine context-dependent functions:

  • Investigate different downstream pathways in various HCC subtypes

  • Examine the influence of the tumor microenvironment on TRIM55 function

  • Consider temporal aspects of TRIM55 activity during disease progression

• Employ multiple complementary methodologies:

  • Use both gain-of-function and loss-of-function approaches

  • Combine in vitro and in vivo models

  • Utilize patient-derived xenografts to better recapitulate human disease complexity

• Validate antibody specificity using TRIM55 knockout controls to ensure observed effects are specific to TRIM55 rather than antibody cross-reactivity .

What are the optimal approaches for studying TRIM55-mediated protein ubiquitination?

To effectively study TRIM55-mediated protein ubiquitination:

• Ubiquitination assay design:

  • In vitro ubiquitination assays using recombinant TRIM55, E1, E2, ubiquitin, and candidate substrates

  • In vivo ubiquitination assays employing co-transfection of TRIM55, ubiquitin (wild-type or mutants to identify specific linkage types), and substrate proteins

• Substrate identification methodology:

  • Use co-immunoprecipitation followed by mass spectrometry

  • Employ proximity-based labeling techniques (BioID or APEX)

  • Screen potential substrates based on bioinformatic prediction of interaction motifs

• Ubiquitin chain analysis:

  • Utilize ubiquitin mutants (K48, K63, etc.) to determine chain topology

  • Employ linkage-specific antibodies for detection

  • Apply mass spectrometry to identify ubiquitination sites and chain types

• Proteasomal degradation analysis:

  • Use proteasome inhibitors (MG132) in conjunction with cycloheximide chase assays

  • Quantify substrate half-life in the presence/absence of TRIM55

  • Confirm proteasome-dependence using both pharmacological and genetic approaches

How can the E3 ligase activity of TRIM55 be measured quantitatively in different experimental systems?

Quantitative measurement of TRIM55 E3 ligase activity can be approached through:

• In vitro reconstitution assays:

  • Prepare recombinant TRIM55 protein with confirmed structural integrity

  • Establish a reaction system with purified E1, appropriate E2 enzymes, ubiquitin, ATP, and substrate proteins

  • Quantify ubiquitin transfer using Western blot or ELISA-based detection

  • Determine enzyme kinetics parameters (Km, Vmax) for TRIM55 activity

• Cellular ubiquitination assays:

  • Develop fluorescent reporter systems using TRIM55 substrate fusion proteins

  • Apply flow cytometry to quantify substrate degradation rates in living cells

  • Implement FRET-based approaches to measure TRIM55-substrate interactions in real-time

• Pharmacological modulation:

  • Test inhibitors of E1, E2, or proteasome to validate the specificity of TRIM55-mediated effects

  • Evaluate TRIM55 activity in response to relevant physiological or pathological stimuli

• Structure-function analysis:

  • Generate TRIM55 mutants affecting the RING domain to disrupt E3 ligase function

  • Create domain-specific deletions to determine the contribution of each domain to substrate recognition and catalytic activity

What are the critical controls for validating TRIM55 antibody specificity in immunoprecipitation experiments?

When validating TRIM55 antibody specificity for immunoprecipitation experiments, implement these critical controls:

• Antibody validation controls:

  • TRIM55 knockout or knockdown lysates as negative controls

  • TRIM55 overexpression lysates as positive controls

  • Pre-adsorption of the antibody with recombinant TRIM55 protein

  • Comparison of results using multiple antibodies targeting different TRIM55 epitopes

• Immunoprecipitation specificity controls:

  • IgG isotype control to assess non-specific binding

  • Reciprocal co-immunoprecipitation to confirm interaction

  • Input control (5-10% of pre-immunoprecipitation lysate)

  • Competitive peptide blocking to confirm epitope specificity

• Binding interaction validation:

  • Salt concentration gradient to assess interaction strength

  • Detergent variation to distinguish direct from indirect interactions

  • RNase/DNase treatment if RNA/DNA-mediated interactions are suspected

  • Use of truncated TRIM55 constructs to map interaction domains

What experimental approaches best reveal the differential roles of TRIM55 across cancer types?

To elucidate the differential roles of TRIM55 across cancer types, researchers should employ:

• Multi-cancer expression profiling:

  • Analyze TRIM55 expression across cancer types using tissue microarrays

  • Correlate expression patterns with clinical parameters and outcomes

  • Compare primary tumors with metastatic samples to assess stage-specific functions

• Target identification in different contexts:

  • Perform immunoprecipitation-mass spectrometry in multiple cancer cell types

  • Compare TRIM55 interactomes across cancer types to identify unique and shared binding partners

  • Validate cancer-specific interactions using co-immunoprecipitation and proximity ligation assays

• Functional impact assessment:

  • Conduct parallel loss-of-function and gain-of-function studies across cancer cell lines

  • Measure effects on proliferation, migration, invasion, and angiogenesis

  • Develop co-culture systems to assess tumor-microenvironment interactions

• Pathway analysis:

  • Perform RNA-seq following TRIM55 modulation in different cancer contexts

  • Use inhibitors of key pathways (NF-κB, c-Myc, HIF1α/VEGF, TGFβ/Smad) to determine their contribution to TRIM55-mediated effects

  • Develop computational models integrating multi-omics data to predict context-dependent functions

How can researchers optimize TRIM55 antibody use for immunohistochemical analysis of clinical samples?

For optimal immunohistochemical analysis using TRIM55 antibodies on clinical samples:

• Sample preparation optimization:

  • Evaluate fixation conditions (duration and fixative type)

  • Compare antigen retrieval methods (heat-induced vs. enzymatic)

  • Test different blocking reagents to minimize background staining

• Antibody validation for IHC:

  • Determine optimal antibody dilution through titration experiments

  • Validate using positive control tissues (skeletal muscle)

  • Include TRIM55-deficient tissues as negative controls

  • Perform peptide competition assays to confirm specificity

• Signal detection optimization:

  • Compare DAB-based and fluorescence-based detection systems

  • Evaluate signal amplification methods for low-expression samples

  • Establish appropriate counterstaining protocols

• Quantification and analysis:

  • Develop standardized scoring systems (H-score, Allred score, etc.)

  • Implement digital pathology tools for quantitative assessment

  • Correlate TRIM55 staining patterns with other biomarkers and clinical parameters

What are the optimal experimental designs for investigating TRIM55's role in the noncanonical NF-κB pathway?

To investigate TRIM55's role in the noncanonical NF-κB pathway, implement these experimental designs:

• Pathway component analysis:

  • Monitor processing of p100 to p52 in response to TRIM55 manipulation

  • Assess phosphorylation status of IKKα

  • Evaluate nuclear translocation of RelB/p52 complexes

  • Measure expression of noncanonical NF-κB target genes

• Ubiquitination analysis:

  • Characterize TRIM55-mediated ubiquitination of p100

  • Determine ubiquitin chain types (K48 vs. K63) using linkage-specific antibodies

  • Identify specific lysine residues on p100 targeted by TRIM55

  • Analyze the role of VCP-UFD1-NPL4 complex formation

• B cell functional assays:

  • Evaluate germinal center formation in TRIM55-deficient mice

  • Assess antibody production following immunization

  • Analyze B cell proliferation, activation, and differentiation

  • Investigate TRIM55's role in B cell-dependent autoimmune models

• Signaling dynamics:

  • Perform time-course experiments following noncanonical NF-κB stimulation

  • Use biosensors to track real-time pathway activation

  • Implement mathematical modeling to understand the kinetics of TRIM55-mediated regulation

What techniques best elucidate the mechanism of TRIM55-mediated regulation of mRNA stability?

To investigate TRIM55's role in regulating mRNA stability:

• RNA-protein interaction analysis:

  • RNA immunoprecipitation (RIP) to assess TRIM55's association with target mRNAs

  • Cross-linking immunoprecipitation (CLIP) to map binding sites with nucleotide resolution

  • RNA electrophoretic mobility shift assays (EMSA) to characterize binding affinities

• mRNA stability measurements:

  • Actinomycin D chase experiments to measure half-lives of target mRNAs

  • Nuclear run-on assays to distinguish effects on transcription from effects on stability

  • Polysome profiling to assess translation efficiency

• Mechanistic investigation:

  • Analyze TRIM55's effect on RNA-binding proteins like NF90

  • Examine ubiquitination status of RNA-binding proteins in response to TRIM55

  • Identify RNA motifs that confer TRIM55-dependent regulation

  • Use mutagenesis to validate functional RNA-protein interaction sites

• High-throughput approaches:

  • RNA-seq with TRIM55 manipulation to identify globally affected transcripts

  • SLAM-seq or similar metabolic labeling techniques to measure synthesis and decay rates

  • Ribosome profiling to assess translation efficiency in a transcriptome-wide manner

How can researchers address nonspecific binding when using TRIM55 antibodies in Western blot?

To minimize nonspecific binding in Western blot using TRIM55 antibodies:

• Antibody quality assessment:

  • Test multiple TRIM55 antibodies targeting different epitopes

  • Validate antibody specificity using TRIM55 knockdown/knockout samples

  • Consider using monoclonal antibodies for higher specificity

• Protocol optimization:

  • Increase blocking time and concentration (5% BSA or milk in TBST)

  • Optimize antibody dilution (start with manufacturer's recommended 1:500-1:2000 range)

  • Increase washing frequency and duration

  • Reduce antibody incubation temperature (4°C overnight rather than room temperature)

• Sample preparation improvements:

  • Ensure complete protein denaturation

  • Add reducing agents to disrupt protein aggregates

  • Pre-clear lysates with Protein A/G beads

  • Optimize SDS-PAGE conditions for better protein separation

• Signal detection optimization:

  • Use highly specific secondary antibodies

  • Implement short exposure times to reduce background

  • Consider using fluorescent secondary antibodies for better quantification

  • Apply digital image acquisition with appropriate dynamic range settings

What strategies can address variability in TRIM55 detection across different tissue types?

To address variability in TRIM55 detection across tissue types:

• Tissue-specific extraction optimization:

  • Adjust lysis buffer composition based on tissue characteristics

  • Develop tissue-specific homogenization protocols

  • Include additional protease inhibitors for tissues with high protease activity

  • Optimize protein extraction temperature and duration

• Detection system adaptation:

  • Adjust antibody concentration based on TRIM55 expression levels in different tissues

  • Implement signal amplification methods for low-expressing tissues

  • Use detection systems with appropriate dynamic range

  • Consider multiplex detection systems to include loading controls

• Normalization strategies:

  • Select appropriate loading controls for each tissue type

  • Implement total protein normalization approaches

  • Apply digital image analysis with appropriate normalization algorithms

  • Use standard curves with recombinant TRIM55 for absolute quantification

• Validation approaches:

  • Confirm findings using orthogonal detection methods

  • Compare results from multiple antibodies targeting different TRIM55 epitopes

  • Include positive control tissues with known TRIM55 expression

  • Validate protein expression with corresponding mRNA analysis

How should researchers interpret contradictory results between TRIM55 transcript and protein levels?

When facing contradictions between TRIM55 transcript and protein levels:

• Regulatory mechanism investigation:

  • Examine post-transcriptional regulation (miRNAs targeting TRIM55 mRNA)

  • Assess post-translational modifications affecting TRIM55 protein stability

  • Investigate autoubiquitination as a potential self-regulatory mechanism

  • Evaluate protein degradation rates using cycloheximide chase assays

• Technical validation:

  • Verify primers specificity for transcript analysis

  • Confirm antibody specificity for protein detection

  • Assess potential isoform-specific detection differences

  • Evaluate sensitivity limits of detection methods

• Biological context consideration:

  • Examine time-dependent relationship between transcript and protein levels

  • Investigate tissue-specific or cell-type-specific regulatory mechanisms

  • Consider disease state or stress conditions affecting translation efficiency

  • Evaluate the impact of the tumor microenvironment on protein stability

• Integrative analysis:

  • Perform parallel measurements at multiple time points

  • Combine transcriptomics, proteomics, and protein turnover studies

  • Develop mathematical models to predict transcript-to-protein relationships

  • Use TRIM55 reporter constructs to monitor real-time regulation

How can TRIM55 antibodies be used to investigate therapeutic potential in cancer?

To investigate TRIM55's therapeutic potential in cancer using antibodies:

• Biomarker development applications:

  • Evaluate TRIM55 expression in patient cohorts using tissue microarrays

  • Correlate expression patterns with treatment response and patient outcomes

  • Develop standardized immunohistochemical protocols for clinical application

  • Assess TRIM55 as part of multi-marker panels for patient stratification

• Mechanism-based therapeutic screening:

  • Use TRIM55 antibodies to monitor pathway activation in drug screening assays

  • Assess drug effects on TRIM55-substrate interactions

  • Evaluate modulation of TRIM55 E3 ligase activity by candidate compounds

  • Screen for compounds that alter TRIM55 protein levels or localization

• Combination therapy assessment:

  • Monitor TRIM55 pathway activation in response to standard therapies

  • Identify synergistic effects between TRIM55 modulation and existing treatments

  • Investigate resistance mechanisms involving TRIM55-regulated pathways

  • Develop rational combination strategies based on TRIM55 mechanistic insights

• Treatment response monitoring:

  • Develop protocols for monitoring TRIM55 activity in patient samples during treatment

  • Create phospho-specific antibodies for TRIM55 or its substrates

  • Implement multiplexed imaging to assess TRIM55 pathway activation in situ

  • Correlate treatment-induced changes in TRIM55 with clinical responses

What methodological approaches best characterize TRIM55's interaction with the ubiquitin-proteasome system?

To characterize TRIM55's interaction with the ubiquitin-proteasome system:

• E2 enzyme partnership identification:

  • Screen E2 enzyme panels for TRIM55 cooperation

  • Perform in vitro ubiquitination assays with purified components

  • Use proximity-based labeling to identify E2 enzymes interacting with TRIM55 in cells

  • Validate functional partnerships through genetic knockdown approaches

• Ubiquitin chain topology analysis:

  • Employ ubiquitin mutants (K48R, K63R, etc.) to determine chain linkage specificity

  • Use linkage-specific antibodies in Western blot analysis

  • Apply mass spectrometry to identify ubiquitination sites and chain compositions

  • Implement in vitro chain assembly assays to determine TRIM55's intrinsic specificity

• Proteasomal targeting mechanism:

  • Assess direct interaction between TRIM55 and proteasome components

  • Evaluate the role of shuttle factors in TRIM55-mediated degradation

  • Use fluorescent reporter systems to track proteasomal degradation dynamics

  • Implement proteasome inhibitors to confirm dependency of TRIM55 effects

• Regulatory feedback mechanisms:

  • Investigate autoubiquitination of TRIM55

  • Assess TRIM55 protein half-life and degradation mechanisms

  • Examine post-translational modifications affecting TRIM55 activity

  • Study the impact of cellular stress conditions on TRIM55-UPS interactions

How can researchers effectively compare TRIM55 function across different model systems?

To effectively compare TRIM55 function across model systems:

• Expression system standardization:

  • Develop consistent protein tagging strategies across models

  • Use identical promoters for transgene expression when possible

  • Quantify expression levels to ensure comparable TRIM55 concentrations

  • Consider inducible expression systems to control timing and level

• Cross-species functional analysis:

  • Perform sequence and structural comparisons of TRIM55 orthologs

  • Conduct complementation studies using species-specific variants

  • Develop species-specific antibodies that recognize conserved epitopes

  • Generate humanized animal models for translational studies

• Phenotypic readout harmonization:

  • Implement standardized assays across different model systems

  • Develop quantitative metrics that can be compared between models

  • Use time-course analyses to align developmental or disease stages

  • Apply systems biology approaches to integrate multi-level data

• Translational correlation:

  • Compare findings from cell lines, animal models, and patient samples

  • Validate key mechanisms across multiple species

  • Develop computational approaches to predict cross-species conservation of function

  • Implement parallel multi-omics profiling across model systems

What are the critical considerations for designing in vivo experiments to study TRIM55 function in cancer models?

When designing in vivo experiments to study TRIM55 function in cancer models:

• Model selection and development:

  • Compare xenograft, syngeneic, and genetically engineered mouse models

  • Consider tissue-specific conditional knockout/knockin approaches

  • Develop inducible systems to study temporal aspects of TRIM55 function

  • Evaluate orthotopic models to maintain appropriate tumor microenvironment

• Endpoint measurement optimization:

  • Implement in vivo imaging for longitudinal tumor growth monitoring

  • Design multiparameter analysis of tumor characteristics (size, invasion, angiogenesis)

  • Develop protocols for circulating tumor cell and metastasis detection

  • Plan comprehensive immunophenotyping of tumor microenvironment

• Intervention timing considerations:

  • Design experiments addressing preventive versus therapeutic interventions

  • Establish protocols for early versus advanced disease stages

  • Consider combination with standard therapies at clinically relevant timing

  • Implement survival analysis with appropriate power calculations

• Analytical validation:

  • Confirm TRIM55 expression/knockout in tumor tissues

  • Verify pathway modulation through molecular and protein analysis

  • Assess pharmacodynamic markers linked to TRIM55 function

  • Correlate in vivo findings with patient data to establish clinical relevance

How might contradictory roles of TRIM55 in different cancers inform precision medicine approaches?

The contradictory roles of TRIM55 across cancer types present both challenges and opportunities for precision medicine:

• Context-dependent biomarker development:

  • Design cancer-specific TRIM55 diagnostic panels

  • Develop algorithms integrating TRIM55 status with other molecular markers

  • Establish threshold values for TRIM55 expression that predict outcomes in each cancer type

  • Create companion diagnostics for TRIM55-targeting therapeutic approaches

• Mechanism-based treatment stratification:

  • Identify molecular signatures that predict TRIM55 function in individual tumors

  • Develop assays measuring activity of TRIM55 downstream pathways

  • Generate patient-derived organoids to test TRIM55-related interventions

  • Implement functional testing of tumor samples for TRIM55-dependent responses

• Dual-targeting strategies:

  • Design approaches simultaneously targeting TRIM55 and its critical substrates

  • Develop context-specific combination therapies based on TRIM55 signaling profiles

  • Create synthetic lethality approaches leveraging TRIM55 status

  • Implement adaptive clinical trial designs incorporating TRIM55 biomarkers

• Treatment resistance considerations:

  • Monitor TRIM55 pathway adaptation during treatment

  • Investigate TRIM55-dependent resistance mechanisms

  • Develop strategies to overcome resistance through TRIM55 pathway modulation

  • Implement longitudinal monitoring of TRIM55 status during treatment

What emerging methodologies might enhance our understanding of TRIM55's role in immune regulation?

Emerging methodologies to enhance understanding of TRIM55's role in immune regulation include:

• Advanced immune cell analysis techniques:

  • Single-cell RNA-seq to identify TRIM55-dependent immune cell subpopulations

  • Mass cytometry (CyTOF) for high-dimensional immune phenotyping

  • Spatial transcriptomics to assess TRIM55 function in tissue microenvironments

  • CRISPR-based genetic screens in primary immune cells

• Advanced imaging approaches:

  • Intravital microscopy to track TRIM55-dependent immune cell dynamics

  • Multiplexed ion beam imaging (MIBI) or imaging mass cytometry for spatial context

  • Live-cell imaging with TRIM55 activity reporters

  • Super-resolution microscopy to study nanoscale organization of signaling complexes

• Systems immunology frameworks:

  • Multi-omics integration of genomic, transcriptomic, and proteomic data

  • Network analysis of TRIM55-dependent signaling in immune contexts

  • Machine learning approaches to identify TRIM55-regulated immune signatures

  • Mathematical modeling of TRIM55's contribution to immune homeostasis

• Humanized immune models:

  • Patient-derived xenografts with humanized immune systems

  • In vitro organoid co-culture systems with autologous immune components

  • Microfluidic organ-on-chip platforms incorporating immune cell dynamics

  • Ex vivo human tissue models maintaining intact immune architecture

How can researchers integrate TRIM55 functional data with broader cancer genomics and proteomics datasets?

To integrate TRIM55 functional data with broader cancer genomics and proteomics datasets:

• Multi-omics data integration:

  • Correlate TRIM55 expression with mutation landscapes across cancer types

  • Identify genomic alterations affecting TRIM55 function or regulation

  • Map TRIM55-dependent ubiquitylome changes using proteomics

  • Correlate transcriptional signatures with TRIM55 activity states

• Network-based analytical approaches:

  • Construct protein-protein interaction networks centered on TRIM55

  • Develop gene regulatory networks incorporating TRIM55 and its targets

  • Implement pathway enrichment analysis for TRIM55-dependent processes

  • Create predictive models of TRIM55 activity based on multi-omics profiles

• Public database integration:

  • Mine cancer genomics databases (TCGA, ICGC) for TRIM55-related patterns

  • Utilize proteomics repositories to validate TRIM55 targets

  • Leverage patient-derived data to establish clinical correlations

  • Implement meta-analysis approaches to identify conserved TRIM55 functions

• Computational tool development:

  • Create algorithms predicting TRIM55 substrates from protein sequence features

  • Develop visualization tools for TRIM55-centered biological networks

  • Generate machine learning models predicting TRIM55 function from multi-omics data

  • Implement text mining approaches to extract TRIM55-related knowledge from literature

What are the most promising therapeutic applications targeting TRIM55 or its regulatory pathways?

The most promising therapeutic applications targeting TRIM55 or its regulatory pathways include:

• Context-specific TRIM55 modulation strategies:

  • Develop inhibitors of TRIM55 E3 ligase activity for gastric cancer and hepatocellular carcinoma contexts where TRIM55 promotes cancer progression

  • Design TRIM55 stabilizers or gene therapy approaches for colorectal cancer contexts where TRIM55 suppresses cancer

  • Create substrate-specific modulators that disrupt or enhance specific TRIM55-substrate interactions

  • Implement combinatorial approaches targeting TRIM55 and its critical partners

• Immune modulation through TRIM55 targeting:

  • Design approaches targeting TRIM55-dependent noncanonical NF-κB signaling for autoimmune diseases

  • Develop B cell-specific TRIM55 modulators for precision immunotherapy

  • Create conditional systems for temporary TRIM55 modulation during immune responses

  • Implement vaccine adjuvants targeting TRIM55-dependent pathways

• Pathway-specific intervention strategies:

  • Target downstream effectors of TRIM55 (c-Myc, HIF1α/VEGF, TGFβ/Smad signaling)

  • Develop approaches modulating TRIM55-regulated RNA stability mechanisms

  • Create combination therapies co-targeting TRIM55 and its substrates

  • Implement synthetic lethality approaches based on TRIM55 status

• Advanced delivery technologies:

  • Design nanoparticle-based delivery of TRIM55 modulators to specific tissues

  • Develop antibody-drug conjugates targeting TRIM55-expressing cells

  • Create cell type-specific TRIM55 modulation using targeted gene editing

  • Implement mRNA-based approaches for temporary TRIM55 modulation