PPIE Antibody, Biotin conjugated

What is PPIE and why is it a significant research target?

PPIE (Peptidyl-prolyl cis-trans isomerase E) is an enzyme involved in protein folding and regulation of RNA processing. It belongs to the cyclophilin family (specifically Cyclophilin-33) and possesses rotamase activity (EC 5.2.1.8), catalyzing the cis-trans isomerization of proline peptide bonds. PPIE is particularly significant in epigenetics and nuclear signaling pathways, making it an important target for researchers studying transcriptional regulation, RNA processing, and related cellular mechanisms. The protein contains specific domains that facilitate interactions with other nuclear proteins and RNA molecules, positioning it as a key player in gene expression regulation. Research with PPIE antibodies helps elucidate these complex cellular processes and their roles in both normal physiology and disease states .

What applications is the biotin-conjugated PPIE antibody suitable for?

• Western blotting for protein detection and quantification

• Immunoprecipitation (IP) for protein isolation

• Immunohistochemistry (IHC) for tissue localization studies

• Immunocytochemistry (ICC) for cellular localization

• Immunofluorescence (IF) when coupled with fluorescent streptavidin conjugates

• Flow cytometry for cell population analysis

The biotin conjugation enables signal amplification through secondary detection with streptavidin or avidin conjugates, which is particularly valuable when detecting low-abundance proteins like transcription factors or regulatory enzymes .

How does the biotin conjugation enhance detection compared to directly labeled antibodies?

Biotin conjugation offers several methodological advantages over directly labeled antibodies. The biotin-streptavidin system provides significant signal amplification because:

• Multiple biotin molecules can be conjugated to a single antibody molecule

• Each streptavidin molecule can bind four biotin molecules with extremely high affinity (Kd ≈ 10^-15 M)

• Streptavidin can be linked to various detection systems (enzymes, fluorophores, etc.)

This creates a multiplying effect where each antibody-antigen interaction generates a much stronger signal than direct labeling approaches. For example, in western blotting or immunohistochemistry, this amplification enables detection of lowly expressed proteins that might be missed with conventional directly labeled antibodies. The system also offers greater flexibility as researchers can choose different streptavidin conjugates (HRP, fluorophores, gold particles) depending on their detection method, without needing different antibody preparations .

What is the recommended storage and handling protocol for maintaining antibody activity?

To maintain optimal activity of the PPIE antibody, biotin conjugated, follow these storage and handling guidelines:

• Upon receipt, store at -20°C or -80°C to prevent degradation

• Avoid repeated freeze-thaw cycles which can compromise antibody activity

• The antibody is supplied in a protective buffer containing 50% glycerol, 0.01M PBS (pH 7.4), and 0.03% Proclin 300 as a preservative

• For working solutions, aliquot the antibody to minimize freeze-thaw cycles

• When diluting, use buffers free of sodium azide if subsequent streptavidin-HRP detection is planned, as azide inhibits peroxidase activity

• Follow appropriate laboratory safety procedures when handling the antibody

Proper storage and handling are crucial for maintaining the binding specificity and signal strength. Researchers should validate antibody performance before critical experiments, particularly after extended storage periods .

What controls should be included when using biotin-conjugated PPIE antibody in experiments?

When designing experiments with biotin-conjugated PPIE antibody, include the following controls to ensure reliable and interpretable results:

• Positive control: Use samples known to express PPIE (human cell lines like HEK293)

• Negative control: Include samples where PPIE is absent or knockdown/knockout models

• Isotype control: Use a biotin-conjugated rabbit IgG antibody not targeting any relevant antigen to assess non-specific binding

• No primary antibody control: Process samples with detection reagents but omit the primary PPIE antibody

• Blocking control: Pre-incubate the antibody with recombinant PPIE protein (immunogen) to verify specificity

• Endogenous biotin control: Block endogenous biotin in samples to prevent background, especially in tissues known to contain high biotin levels

• Competitive binding control: As demonstrated in Drug-ID experiments, include excess non-conjugated target to verify specific binding

These controls help differentiate between true positive signals and experimental artifacts. For example, in western blot applications, blocking with the immunogen should eliminate the 53 kD band seen with phospho-specific antibodies in similar experimental setups .

How should sample preparation be optimized for PPIE detection in different experimental contexts?

Sample preparation methods should be tailored to the specific application and experimental context:

For ELISA:

• Prepare cell or tissue lysates using RIPA or NP-40 buffer containing protease inhibitors

• Standardize protein concentration (typically 1-10 μg/mL)

• For phosphorylation studies, include phosphatase inhibitors in all buffers

• Optimize coating conditions (pH, buffer, concentration)

For Western Blotting:

• Use RIPA or NP-40 lysis buffers with protease/phosphatase inhibitors

• Load 25-125 μg protein per lane (based on target abundance)

• Transfer proteins to appropriate membrane (PVDF or nitrocellulose)

• Block with BSA-based blockers rather than milk for phosphoprotein detection

• Include denaturing agents (SDS, heat) to expose epitopes

For Immunoprecipitation:

• Use gentler lysis conditions (NP-40 or Triton X-100 buffers)

• Pre-clear lysates with protein G beads to reduce non-specific binding

• Optimize antibody:antigen ratio (typically 2-5 μg antibody per 500 μg protein)

• Include appropriate controls (IgG, input)

For all applications, consider cell treatment conditions that might affect PPIE expression or modification, such as stimulation with growth factors or stress inducers like UV treatment (50-400 J) or phosphatase inhibitors like okadaic acid (0.1 μM) .

How can researchers validate the specificity of their PPIE antibody detection system?

Validating antibody specificity is critical for reliable research. For PPIE antibody, implement these complementary validation approaches:

• Genetic validation: Compare detection between wild-type and PPIE knockdown/knockout systems

• Immunogen blocking: Pre-incubate the antibody with excess PPIE recombinant protein (specifically the 86-141AA region used as immunogen)

• Orthogonal detection: Confirm findings with alternative antibodies targeting different PPIE epitopes

• Expression profile correlation: Compare detection patterns with known PPIE mRNA expression data

• Molecular weight verification: Confirm detection at the expected molecular weight (~33 kDa for PPIE)

• Immunoprecipitation-Mass Spectrometry: Perform IP followed by MS to confirm identity of captured proteins

• Recombinant protein controls: Test antibody against purified recombinant PPIE protein

For antibodies detecting post-translational modifications, additional controls should include:

• Treatment with appropriate enzymes (phosphatases for phosphorylation)

• Stimulation/inhibition experiments altering the modification state

• Comparison with site-specific antibodies

Document validation thoroughly in laboratory records and publications to support reproducibility and reliability of findings .

How can biotin-conjugated PPIE antibody be incorporated into multi-color immunofluorescence protocols?

Incorporating biotin-conjugated PPIE antibody into multi-color immunofluorescence requires careful planning to avoid cross-reactivity and maximize signal separation:

• Sequential detection protocol:

  • Apply primary antibodies sequentially rather than simultaneously

  • Block between detection steps with avidin/biotin blocking kit

  • Use spectrally distinct fluorophores conjugated to streptavidin (e.g., Alexa Fluor 488, 594, 647)

• Multiplexing strategy:

  • Combine the biotin-PPIE antibody with directly labeled antibodies from different species

  • Example workflow: Apply biotin-PPIE antibody (rabbit) → Block → Apply mouse anti-protein X → Apply goat anti-protein Y → Detect with streptavidin-AF488 + anti-mouse-AF594 + anti-goat-AF647

• Signal amplification for low-abundance targets:

  • Use tyramide signal amplification (TSA) with the biotin-streptavidin system

  • Apply streptavidin-HRP after biotin-PPIE antibody

  • React with tyramide-fluorophore for covalent signal deposition

  • This permits antibody stripping while preserving signal for subsequent rounds

• Optimization parameters:

  • Antibody dilution (typically 1:100-1:500)

  • Incubation time and temperature

  • Washing stringency

  • Order of antibody application

This approach enables co-localization studies between PPIE and other proteins of interest, such as RNA processing factors or nuclear structural proteins, providing insights into functional interactions within cellular compartments .

What are effective approaches for troubleshooting high background when using biotin-conjugated antibodies?

High background is a common challenge with biotin-conjugated antibodies. Implement these methodological solutions:

• Endogenous biotin blocking:

  • Use commercial avidin/biotin blocking kits

  • Apply free avidin to block endogenous biotin, followed by biotin to saturate remaining avidin binding sites

  • Particularly important for biotin-rich tissues (liver, kidney, brain)

• Optimization of blocking conditions:

  • Use 2-5% BSA instead of milk-based blockers (milk contains biotin)

  • Add 0.1-0.3% Triton X-100 or Tween-20 to reduce hydrophobic interactions

  • Consider specialized blockers containing immunoglobulin-blocking proteins

• Sample preparation improvements:

  • Increase washing duration and frequency (4-6 washes of 5-10 minutes each)

  • Perfuse tissues thoroughly if using in vivo samples

  • Use freshly prepared fixatives and optimize fixation time

• Reagent-specific adjustments:

  • Titrate antibody concentration (perform serial dilutions)

  • Reduce streptavidin-conjugate concentration

  • Switch to more specific detection systems (e.g., streptavidin polymers)

  • Filter solutions to remove aggregates

• Protocol modifications:

  • Perform incubations at 4°C overnight instead of room temperature

  • Pre-absorb antibody with tissue/cell powder from negative control samples

  • Include 5-10% serum from the host species of your secondary reagent

Systematic documentation of optimization steps helps identify the specific source of background in your experimental system .

How can proximity biotinylation be combined with PPIE antibody for studying protein-protein interactions?

Combining proximity biotinylation with PPIE antibody creates powerful tools for mapping protein-protein interactions in living cells:

• BioID approach:

  • Generate expression constructs fusing PPIE with a promiscuous biotin ligase (BirA*)

  • Express in target cells and supply biotin (50 μM for 16-24 hours)

  • The BirA* enzyme will biotinylate proteins within ~10 nm radius of PPIE

  • Lyse cells and capture biotinylated proteins with streptavidin

  • Identify interaction partners by mass spectrometry

• APEX2 system for temporal resolution:

  • Fuse PPIE with APEX2 peroxidase

  • Add biotin-phenol substrate and H₂O₂ for short pulse labeling (1 minute)

  • This approach provides temporal resolution for dynamic interactions

• Drug-ID methodology adaptation:

  • Similar to the approach described in search result

  • Create a chemical conjugate between a PPIE-binding molecule and biotin ligase

  • This allows biotinylation of proteins interacting with PPIE in native contexts

  • Particularly useful when direct fusion might disrupt protein function

• Validation with conventional approaches:

  • Confirm key interactions with co-immunoprecipitation using anti-PPIE antibody

  • Perform reciprocal IP experiments

  • Validate with orthogonal methods (FRET, PLA, etc.)

This methodology could reveal PPIE's role in RNA processing complexes, potentially identifying interactions with splicing regulators, RNA helicases, or chromatin modifiers relevant to its function in epigenetic regulation .

What are the considerations for quantitative analysis of PPIE expression or modification using biotin-conjugated antibodies?

Quantitative analysis using biotin-conjugated PPIE antibody requires careful attention to experimental design and data analysis:

• Signal linearity assessment:

  • Generate standard curves using recombinant PPIE at known concentrations

  • Determine the linear range of detection for accurate quantification

  • Typical linear range spans 2-3 orders of magnitude

• Normalization strategies:

  • For western blots: normalize to housekeeping proteins (β-actin, GAPDH)

  • For cellular assays: normalize to cell number or total protein

  • For tissue sections: normalize to tissue area or nuclear count

  • Consider the use of spike-in standards for absolute quantification

• Signal amplification considerations:

  • The biotin-streptavidin system provides non-linear signal amplification

  • Calibrate the relationship between protein quantity and signal intensity

  • Avoid detection saturation which compromises quantification

  • Use densitometry software with appropriate background correction

• Statistical approach:

  • Perform experiments with sufficient biological replicates (n≥3)

  • Apply appropriate statistical tests based on data distribution

  • Report variability measures (standard deviation, standard error)

  • Consider power analysis to determine sample size requirements

• Technical recommendations:

  • Maintain consistent exposure times between experimental comparisons

  • Include internal calibration standards on each gel/plate

  • Use automated image analysis to reduce subjective bias

  • Document all analysis parameters for reproducibility

These approaches enable reliable quantitative comparisons of PPIE expression or modification states between experimental conditions, such as different cell treatments, tissue types, or disease models .

How does biotin-conjugated antibody detection compare with other detection systems for studying PPIE?

Different detection methodologies offer distinct advantages and limitations for PPIE research:

Biotin-conjugated antibody detection provides strong signal amplification advantages, particularly useful for:

• Detecting low-abundance nuclear proteins like PPIE

• Applications requiring high sensitivity but where spatial information is important

• Systems where multiplexing requirements are modest

• Absolute quantification is critical (MS-based methods preferable)

• Highly multiplexed detection is needed (direct fluorophore conjugation or mass cytometry)

• Concerns about endogenous biotin interference exist (direct conjugation methods)

The biotin-streptavidin system remains particularly valuable for immunohistochemistry and western blotting applications where its signal amplification properties enhance detection of nuclear factors like PPIE .

What experimental approaches combine PPIE antibody detection with functional assays of enzymatic activity?

Combining antibody detection with functional assays provides comprehensive insights into PPIE biology:

• Immunocapture followed by rotamase activity assay:

  • Immobilize biotin-PPIE antibody on streptavidin-coated surfaces

  • Capture PPIE from cell/tissue lysates

  • Measure rotamase (PPIase) activity using chromogenic or fluorogenic peptide substrates

  • Quantify catalytic activity (Kcat/Km) under different experimental conditions

• In situ activity correlation:

  • Perform immunostaining for PPIE localization using biotin-PPIE antibody

  • In parallel samples, conduct activity-based protein profiling with activity probes

  • Correlate spatial distribution of PPIE protein with enzymatic activity

• Pull-down combined with substrate binding assays:

  • Use biotin-PPIE antibody to isolate protein complexes

  • Analyze binding to potential RNA substrates using EMSA or RNA immunoprecipitation

  • Correlate binding with functional outcomes in cellular assays

• Integrated phosphorylation analysis:

  • Combine biotin-PPIE antibody with phospho-specific antibodies

  • Determine how phosphorylation state correlates with enzymatic activity

  • Analyze effects of treatments like UV irradiation (50-400 J) or phosphatase inhibitors like okadaic acid (0.1 μM)

These integrated approaches connect PPIE's presence and modifications to its functional roles in cellular contexts, providing mechanistic insights beyond simple protein detection .

How can researchers design experiments to study post-translational modifications of PPIE using biotin-conjugated antibodies?

Post-translational modifications (PTMs) study requires specialized experimental design:

• Sequential immunoprecipitation approach:

  • First IP: Use biotin-PPIE antibody to capture total PPIE protein

  • Elution under mild conditions to preserve modifications

  • Second IP: Use modification-specific antibodies (e.g., anti-phosphoserine)

  • Alternatively, analyze first IP eluate by western blot with modification-specific antibodies

• Modification-specific enrichment workflow:

  • Enrich for specific modifications first (e.g., phosphopeptide enrichment)

  • Then detect PPIE in the enriched fraction using biotin-PPIE antibody

  • This approach is particularly useful for low-abundance modifications

• Mass spectrometry integration:

  • Capture PPIE using biotin-PPIE antibody and streptavidin beads

  • Process for MS analysis with PTM-friendly protocols

  • Use SILAC or TMT labeling for quantitative comparison between conditions

  • Analyze data with PTM-focused search algorithms

• Validation experiments:

  • Mutate potential modification sites and assess functional consequences

  • Use pharmacological modulators of modifying enzymes

  • Apply specific phosphatase treatments to confirm phosphorylation signals

  • Compare results with phospho-specific antibodies like anti-phosphoserine or anti-phosphotyrosine

• Physiological induction of modifications:

  • Treat cells with stimuli known to induce specific modifications

  • Compare treatment conditions (e.g., UV exposure at 0-400 J or okadaic acid at 0.1 μM)

  • Correlate modification status with functional outcomes

This systematic approach enables characterization of how PTMs regulate PPIE function in epigenetic and nuclear signaling pathways .

What are the methodological considerations for using biotin-conjugated PPIE antibody in live-cell imaging applications?

Live-cell imaging with biotin-conjugated antibodies presents unique challenges requiring specialized approaches:

• Cell permeabilization strategies:

  • Use mild detergents (0.01% saponin, 0.001% digitonin)

  • Apply pore-forming toxins (streptolysin O) at optimized concentrations

  • Employ cell-penetrating peptide conjugates to deliver antibodies

  • These methods must balance membrane permeability with cell viability

• Detection system optimization:

  • Use streptavidin conjugated to bright, photostable fluorophores (Alexa Fluor 488, 568, 647)

  • Consider quantum dots for extended imaging with reduced photobleaching

  • Optimize signal-to-noise ratio through background reduction techniques

  • Minimize phototoxicity with reduced laser power and antifade reagents

• Temporal considerations:

  • Design pulse-chase experiments to track PPIE dynamics

  • Establish time windows that balance antibody penetration with cell viability

  • Consider photoactivatable or photoswitchable probes for precise temporal control

• Alternative detection strategies:

  • Use biotin-conjugated Fab fragments for reduced size and better penetration

  • Consider nanobody-based detection systems if available

  • Complement antibody approaches with genetically encoded tags when possible

• Controls and validation:

  • Include membrane integrity assays to ensure cell viability

  • Perform parallel fixed-cell experiments to validate observations

  • Use fluorescence recovery after photobleaching (FRAP) to assess mobility

  • Confirm specificity with competition experiments using excess unconjugated antibody

While challenging, these approaches can provide unique insights into PPIE dynamics in nuclear compartments, potentially revealing its role in real-time RNA processing events or responses to cellular stressors .

How can PPIE antibodies be applied to study its role in RNA processing and epigenetic regulation?

PPIE's dual role in RNA processing and epigenetic regulation can be investigated through several strategic approaches:

• Chromatin immunoprecipitation (ChIP) applications:

  • Use biotin-PPIE antibody to perform ChIP-seq experiments

  • Map PPIE binding sites across the genome

  • Correlate with histone modification patterns and transcription factor binding

  • Analyze enrichment at specific genomic features (promoters, enhancers, splice sites)

• RNA-protein interaction studies:

  • Adapt CLIP (Cross-Linking and Immunoprecipitation) protocols using biotin-PPIE antibody

  • Identify RNA targets bound by PPIE in vivo

  • Analyze binding motifs and RNA structural preferences

  • Correlate with alternative splicing patterns or RNA stability

• Functional nuclear domain localization:

  • Use biotin-PPIE antibody with streptavidin-fluorophores for high-resolution imaging

  • Co-stain with markers of nuclear domains (splicing speckles, Cajal bodies)

  • Apply super-resolution microscopy techniques to resolve subnuclear localization

  • Analyze dynamics following transcriptional inhibition or stimulation

• Protein complex analysis:

  • Perform immunoprecipitation with biotin-PPIE antibody

  • Identify interacting partners through mass spectrometry

  • Focus on interactions with histone modifiers, chromatin remodelers, and splicing factors

  • Validate key interactions through reciprocal immunoprecipitation

These methodologies can reveal how PPIE coordinates RNA processing with chromatin state, potentially uncovering mechanisms by which post-transcriptional regulation interfaces with epigenetic control .

What approaches can be used to study PPIE in disease models using biotin-conjugated antibodies?

Studying PPIE in disease contexts requires specialized experimental designs:

• Clinical sample analysis workflow:

  • Collect matched disease and control tissues/biopsies

  • Prepare tissue microarrays for high-throughput screening

  • Perform immunohistochemistry with biotin-PPIE antibody

  • Quantify expression levels, subcellular localization, and correlation with disease markers

  • Validate findings with orthogonal methods (qPCR, western blot)

• Cellular disease model characterization:

  • Establish relevant cell culture models (patient-derived cells, genetic models)

  • Analyze PPIE expression, localization, and modification using biotin-PPIE antibody

  • Compare with wild-type controls under basal and stressed conditions

  • Correlate changes with functional readouts (gene expression, splicing patterns)

• Therapeutic response monitoring:

  • Treat disease models with candidate compounds

  • Track PPIE expression, localization, and activity before and after treatment

  • Use biotin-PPIE antibody in multiplexed assays with disease markers

  • Correlate PPIE status with treatment outcomes

• Biomarker development pipeline:

  • Assess PPIE as a potential biomarker through systematic analysis

  • Develop standardized protocols for biotin-PPIE antibody in diagnostic applications

  • Establish quantitative thresholds for clinical relevance

  • Validate across multiple patient cohorts with appropriate controls

These approaches can illuminate PPIE's potential roles in diseases involving disrupted RNA processing or epigenetic dysregulation, such as certain cancers or neurodegenerative disorders where nuclear functions are compromised .

How can researchers adapt high-throughput screening methodologies using biotin-conjugated PPIE antibody?

High-throughput screening with biotin-PPIE antibody enables large-scale studies:

• Automated ELISA platform development:

  • Optimize biotin-PPIE antibody concentration for 96/384-well formats

  • Standardize detection with streptavidin-HRP or fluorescent conjugates

  • Develop robust positive and negative controls for plate validation

  • Implement quality control metrics (Z-factor, signal-to-background ratio)

• Cell-based high-content screening approach:

  • Establish cell models in multi-well imaging plates

  • Optimize fixation, permeabilization, and staining protocols

  • Use biotin-PPIE antibody with fluorescent streptavidin for detection

  • Implement automated image acquisition and analysis for:

    • PPIE expression levels

    • Nuclear/cytoplasmic distribution

    • Co-localization with marker proteins

    • Morphological features

• Compound screening protocol:

  • Treat cells with compound libraries in dose-response format

  • Detect changes in PPIE expression, localization, or modification

  • Include appropriate controls (vehicle, positive modulators)

  • Develop analysis pipelines to identify hits affecting PPIE biology

• Functional genetic screens integration:

  • Combine with CRISPR, RNAi, or cDNA overexpression libraries

  • Use biotin-PPIE antibody to detect phenotypic consequences

  • Correlate genetic perturbations with PPIE pathway alterations

  • Validate hits with secondary assays

This systematic approach enables discovery of compounds or genes that modulate PPIE function, potentially identifying novel regulators of RNA processing and epigenetic pathways relevant to both basic research and therapeutic development .

What are the current limitations of biotin-conjugated PPIE antibody research and potential future improvements?

Current limitations and future directions for biotin-conjugated PPIE antibody applications include several methodological and technical considerations:

• Current technical limitations:

  • Batch-to-batch variability in antibody performance

  • Limited epitope coverage with single antibody reagents

  • Background signals from endogenous biotin in certain tissues

  • Cross-reactivity potential with related cyclophilin family members

  • Challenges in quantitative standardization across laboratories

• Emerging antibody technologies:

  • Development of recombinant antibody formats with improved consistency

  • Single-domain antibodies (nanobodies) for improved tissue penetration

  • Site-specific biotin conjugation for optimal antigen binding

  • Photoactivatable antibody conjugates for spatiotemporal control

  • Bifunctional antibodies combining PPIE targeting with proximity labeling

• Integration with advanced research technologies:

  • Combining with CRISPR-based genomic engineering for endogenous tagging

  • Application in spatial transcriptomics and proteomics platforms

  • Incorporation into microfluidic and organ-on-chip technologies

  • Development of antibody-based biosensors for real-time monitoring

• Standardization initiatives:

  • Establishment of reference standards for antibody validation

  • Development of quantitative calibrators for cross-laboratory comparisons

  • Open-source sharing of optimized protocols and validation data

  • Integration with antibody validation databases and resources

These developments will enhance the reliability, reproducibility, and utility of biotin-conjugated PPIE antibodies, enabling more sophisticated investigations of this important regulatory protein in diverse experimental contexts .

What future research questions about PPIE could be addressed using biotin-conjugated antibodies?

Biotin-conjugated PPIE antibodies can facilitate investigation of several compelling research questions:

• Mechanistic questions at molecular level:

  • How do post-translational modifications regulate PPIE's enzymatic activity and interactions?

  • What is the dynamic interplay between PPIE and chromatin-modifying complexes?

  • How does PPIE contribute to co-transcriptional RNA processing decisions?

  • What structural changes occur in PPIE upon substrate binding?

• Cellular process investigations:

  • How does PPIE localization change during cell cycle progression?

  • What is PPIE's role in stress-responsive RNA processing mechanisms?

  • How do cytoplasmic and nuclear pools of PPIE communicate and regulate each other?

  • What triggers PPIE redistribution between different nuclear compartments?

• Physiological and disease-related inquiries:

  • How does PPIE expression and function change during development and differentiation?

  • What is PPIE's potential role in neurodegenerative diseases with RNA processing defects?

  • How might PPIE contribute to cancer progression through epigenetic mechanisms?

  • Could PPIE serve as a biomarker for diseases with altered RNA processing?

• Therapeutic exploration:

  • Can targeted modulation of PPIE activity affect disease-relevant RNA processing events?

  • What compounds effectively and specifically modulate PPIE function?

  • How do existing RNA-targeting therapeutics affect PPIE-dependent processes?

  • Could PPIE inhibition synergize with other epigenetic therapies?