DPYSL2 Antibody

What is DPYSL2 and why is it an important research target?

DPYSL2 (dihydropyrimidinase-like 2) is a cytoplasmic protein of 572 amino acid residues with a mass of 62.3 kDa. It belongs to the Hydantoinase/dihydropyrimidinase protein family and plays critical roles in neuronal development and polarity, axon growth and guidance, neuronal growth cone collapse, and cell migration. DPYSL2 is also known by several synonyms including CRMP2, DHPRP2, DRP-2, DRP2, N2A3, ULIP-2, ULIP2, and CRMP-2. Its ubiquitous expression across many tissue types and involvement in multiple cellular processes make it an important target for research in both normal development and disease states .

The protein has gained significant attention due to its emerging roles in various cancer types, including acute myeloid leukemia and bladder cancer, where it has been identified as a potential therapeutic target and prognostic marker .

What are the most common applications for DPYSL2 antibodies in research?

DPYSL2 antibodies are utilized in multiple experimental applications, with the following being most commonly employed:

• Western Blot (WB): The most widely used application for detecting DPYSL2 protein expression levels and post-translational modifications

• Enzyme-Linked Immunosorbent Assay (ELISA): For quantitative measurement of DPYSL2 in samples

• Immunofluorescence (IF): For visualizing subcellular localization and co-localization studies

• Immunohistochemistry (IHC): For examining expression patterns in tissue samples

• Immunoprecipitation (IP): For studying protein-protein interactions involving DPYSL2

These techniques have been referenced in over 170 scientific publications, demonstrating their reliability and widespread acceptance in the research community .

How should researchers select the appropriate DPYSL2 antibody for their specific application?

When selecting a DPYSL2 antibody for research, consider the following criteria:

• Application compatibility: Verify that the antibody has been validated for your specific application (WB, IHC, IF, etc.)

• Species reactivity: Ensure cross-reactivity with your experimental model organism (human, mouse, rat, etc.)

• Epitope recognition: Select antibodies targeting different epitopes based on:

  • Full-length protein recognition for expression studies

  • Isoform-specific epitopes if studying particular variants

  • Phospho-specific antibodies for studying post-translational modifications

• Clonality: Consider monoclonal antibodies for high specificity or polyclonal antibodies for stronger signals

• Validation data: Review published literature and manufacturer validation data showing antibody performance

For challenging applications, consider using multiple antibodies recognizing different epitopes to confirm findings and reduce the risk of non-specific binding .

What controls should be included when using DPYSL2 antibodies in experimental setups?

A robust experimental design using DPYSL2 antibodies should include the following controls:

• Positive controls:

  • Cell lines or tissues with confirmed DPYSL2 expression (neuronal tissues show high expression)

  • Recombinant DPYSL2 protein for Western blot

  • Transfected cells overexpressing DPYSL2

• Negative controls:

  • DPYSL2 knockdown samples using validated shRNA (sequences available: Control 5′-ACAGAAGCGATTGTTGATC-3′, DPYSL2 sh1 5′-GGCTTTCAAAGATCGCTTCCA-3′, DPYSL2 sh2 5′-CCTACACATCTATGGGTATCA-3′)

  • Tissues with minimal DPYSL2 expression

  • Secondary antibody-only controls

• Specificity controls:

  • Blocking peptide competition assays

  • Multiple antibodies targeting different epitopes

  • Knockout/knockdown validation

These controls help distinguish true signals from background noise and confirm antibody specificity, enhancing the reliability of experimental results .

What are the optimal sample preparation methods for detecting DPYSL2 in different applications?

Optimal sample preparation varies by application:

For Western Blot:

• Extract proteins using RIPA buffer supplemented with protease and phosphatase inhibitors

• Include 1% NP-40 or Triton X-100 to enhance solubilization

• Sonicate briefly to break down DNA

• Heat samples at 95°C for 5 minutes in Laemmli buffer

• Load 20-50 μg total protein per lane

For Immunohistochemistry:

• Fix tissues in 4% paraformaldehyde for 24 hours

• Use citrate buffer (pH 6.0) for antigen retrieval

• Block with 5% normal serum from the same species as the secondary antibody

• Optimize primary antibody concentration (typically 1:100 to 1:500 dilution)

• Include antigen retrieval steps to expose epitopes

For Immunofluorescence:

• Fix cells in 4% paraformaldehyde for 15 minutes at room temperature

• Permeabilize with 0.2% Triton X-100 for 10 minutes

• Block with 3% BSA for at least 1 hour

• Incubate with primary antibody overnight at 4°C

• Use fluorophore-conjugated secondary antibodies with minimal spectral overlap if performing co-localization studies

How can researchers troubleshoot common issues with DPYSL2 antibody experiments?

For optimal results, validate new antibody lots by comparing them with previously validated antibodies using the same experimental conditions .

What reference datasets exist for DPYSL2 expression across different tissues and cell types?

Multiple reference datasets provide valuable information on DPYSL2 expression patterns:

• Tissue expression patterns: DPYSL2 is ubiquitously expressed across many tissue types with particularly high expression in neuronal tissues.

• Cell line reference data: Various cell line databases document DPYSL2 expression, which can be useful for selecting appropriate positive control cell lines for antibody validation.

• Cancer expression databases: Public databases such as GEPIA show that AML patients have higher DPYSL2 mRNA levels than normal samples, providing valuable comparison points for researchers studying DPYSL2 in cancer contexts .

• Normal vs. pathological expression: Studies have demonstrated that DPYSL2 expression is upregulated in bladder cancer tissue compared with adjacent normal bladder tissue, and expression correlates with cancer staging .

• Subcellular localization: The canonical localization of DPYSL2 is cytoplasmic, though changes in localization can occur under specific cellular conditions .

These reference datasets provide crucial benchmarks for researcher validation and experimental design.

What is known about the role of DPYSL2 in cancer progression and how can antibodies help elucidate these mechanisms?

DPYSL2 has emerging roles in cancer biology with significant implications for disease progression:

DPYSL2 antibodies facilitate these discoveries through:

• Expression profiling using IHC and Western blot to correlate DPYSL2 levels with clinical outcomes

• Co-immunoprecipitation to identify protein interaction partners like PKM2

• Immunofluorescence to track subcellular localization changes during disease progression

• Phospho-specific antibodies to monitor activation of signaling pathways

These applications have helped establish DPYSL2 as a potential therapeutic target for cancer treatment .

How can researchers effectively use DPYSL2 antibodies in studies of drug resistance mechanisms?

DPYSL2 has been identified as a potential mediator of drug resistance, particularly in the context of homoharringtonine (HHT) resistance in AML. Researchers can effectively use DPYSL2 antibodies to study drug resistance through several approaches:

• Expression monitoring: Use Western blot to track DPYSL2 protein levels before and after drug treatment. Studies have shown that DPYSL2 protein levels decreased in three AML cell lines following HHT treatment .

• Target validation studies: DPYSL2 was identified as a differentially expressed gene between HHT-resistant and HHT-sensitive cells by RNA-seq. Antibodies can confirm these findings at the protein level .

• Mechanism exploration: Auto-docking studies revealed that HHT can target DPYSL2, forming a hydrogen bond with the ARG-173 residue with a binding energy of -3.83. Antibodies specific to this region can help validate structural interactions .

• Treatment response monitoring: Dynamic expression analysis using DPYSL2 antibodies can track protein level changes during treatment. mRNA expression analyses have shown that DPYSL2 levels were reduced after complete remission in AML patients with high DPYSL2 expression at diagnosis .

• In vivo validation: Antibodies can be used to confirm knockdown efficiency in xenograft models studying the effects of DPYSL2 inhibition on drug sensitivity and tumor growth .

These approaches help elucidate the molecular mechanisms of drug resistance and identify strategies to overcome therapeutic challenges.

What are the recommended protocols for studying DPYSL2 interactions with other proteins?

To study DPYSL2 protein-protein interactions, researchers should consider the following approaches:

• Co-immunoprecipitation (Co-IP):

  • Lyse cells in a gentle buffer (e.g., 25 mM Tris-HCl pH 7.4, 150 mM NaCl, 1% NP-40, 1 mM EDTA, protease inhibitors)

  • Pre-clear lysate with protein A/G beads

  • Incubate with DPYSL2 antibody (5-10 μg per mg of protein) overnight at 4°C

  • Add protein A/G beads for 2-3 hours

  • Wash 4-5 times with buffer containing reduced detergent

  • Elute with Laemmli buffer and analyze by Western blot using antibodies against suspected interaction partners

• Proximity Ligation Assay (PLA):

  • Fix cells with 4% paraformaldehyde

  • Permeabilize with 0.2% Triton X-100

  • Incubate with primary antibodies against DPYSL2 and the target protein (from different species)

  • Apply species-specific PLA probes

  • Perform ligation and amplification according to manufacturer's protocol

  • Visualize interaction signals by fluorescence microscopy

• Bimolecular Fluorescence Complementation (BiFC):

  • Clone DPYSL2 and potential interacting protein with split fluorescent protein fragments

  • Transfect constructs into appropriate cell lines

  • Analyze reconstituted fluorescence indicating protein-protein interaction

These methods have successfully identified that DPYSL2 interacts with pyruvate kinase M2 (PKM2) in bladder cancer cells, promoting the conversion of PKM2 tetramers to PKM2 dimers, which enhances aerobic glycolysis and epithelial-mesenchymal transition .

How do post-translational modifications of DPYSL2 affect its function, and how can these be studied?

DPYSL2 undergoes several post-translational modifications (PTMs) that significantly impact its function in various cellular processes. Studying these modifications requires specialized approaches:

• Phosphorylation sites:

  • Multiple kinases phosphorylate DPYSL2, affecting its roles in cytoskeletal dynamics and signaling

  • Use phospho-specific antibodies to detect site-specific phosphorylation

  • Employ phos-tag gels to separate phosphorylated from non-phosphorylated forms

  • Confirm with mass spectrometry for precise mapping of phosphorylation sites

• SUMOylation and ubiquitination:

  • Affect DPYSL2 stability and subcellular localization

  • Use co-IP with SUMO or ubiquitin antibodies to detect modified forms

  • Employ proteasome inhibitors to stabilize ubiquitinated forms

  • Analyze by Western blot with DPYSL2 antibodies to detect higher molecular weight bands

• Glycosylation:

  • Can impact DPYSL2 folding and function

  • Treat samples with glycosidases and analyze mobility shifts by Western blot

  • Use lectin-based enrichment followed by DPYSL2 antibody detection

• Methodological approach:

  • Compare PTM patterns between normal and disease states using phospho-specific antibodies

  • Use kinase inhibitors to manipulate phosphorylation status

  • Create site-specific mutants to study functional consequences of specific modifications

  • Employ mass spectrometry for comprehensive PTM profiling

Understanding these modifications is critical as they may play roles in DPYSL2's involvement in disease processes, including its function in the JAK2/STAT3/STAT5-PI3K P85/AKT/GSK3b signaling axis in AML .

What experimental approaches are recommended for studying DPYSL2's role in cellular metabolism?

Recent research has revealed DPYSL2's unexpected role in cellular metabolism, particularly in cancer. To investigate this function, the following approaches are recommended:

• Glucose uptake assays:

  • Use fluorescent glucose analogs (2-NBDG) to measure uptake rates in cells with manipulated DPYSL2 levels

  • Compare glucose uptake between control and DPYSL2-knockdown cells using radioactive glucose

  • Studies have shown that DPYSL2 affects glucose uptake in bladder cancer cells

• Lactate production measurement:

  • Quantify extracellular lactate levels using enzymatic assays or lactate meters

  • Compare lactate production in cells with normal vs. altered DPYSL2 expression

  • Research has demonstrated that DPYSL2 promotes lactic acid production in cancer cells

• Metabolic enzyme activity assays:

  • Measure pyruvate kinase M2 (PKM2) activity in the presence and absence of DPYSL2

  • Assess the ratio of PKM2 tetramers to dimers using native gel electrophoresis

  • DPYSL2 has been shown to promote the conversion of PKM2 tetramers to PKM2 dimers

• Seahorse metabolic analysis:

  • Measure oxygen consumption rate (OCR) and extracellular acidification rate (ECAR)

  • Compare glycolytic capacity and mitochondrial function between control and DPYSL2-modified cells

• Metabolomics profiling:

  • Use mass spectrometry to generate comprehensive metabolite profiles

  • Compare metabolite levels between control and DPYSL2-knockdown cells

• In vivo validation:

  • Use PET imaging with 18F-FDG to assess glucose uptake in xenograft tumors with modified DPYSL2 expression

These approaches have helped establish that DPYSL2 promotes aerobic glycolysis in cancer cells through its interaction with PKM2, contributing to the Warburg effect that supports cancer progression .

How can researchers investigate DPYSL2's role in epithelial-mesenchymal transition (EMT)?

DPYSL2 has been implicated in promoting epithelial-mesenchymal transition (EMT) in cancer cells. To investigate this role, researchers should consider these methodological approaches:

• EMT marker analysis:

  • Use Western blot with antibodies against epithelial markers (E-cadherin, ZO-1) and mesenchymal markers (N-cadherin, Vimentin, Snail, Slug, Twist)

  • Compare marker expression in cells with normal vs. altered DPYSL2 levels

  • Perform immunofluorescence to visualize changes in marker localization and expression

  • Quantitative analysis of these markers can reveal the extent of EMT induction or suppression

• Cell migration and invasion assays:

  • Conduct wound healing/scratch assays to assess migration capacity

  • Use Transwell chambers with or without Matrigel coating to evaluate invasion potential

  • Compare migration/invasion between control and DPYSL2-knockdown cells

  • Time-lapse microscopy can provide dynamic insights into migratory behavior changes

• Morphological analysis:

  • Document and quantify morphological changes associated with EMT using phase-contrast microscopy

  • Perform cytoskeletal staining (F-actin) to visualize structural reorganization

• Transcriptional regulation:

  • Use ChIP assays to study binding of EMT-related transcription factors to target promoters

  • Conduct reporter assays to measure activity of EMT-related promoters

  • Perform RT-qPCR to quantify mRNA levels of EMT markers

• Rescue experiments:

  • Knockdown PKM2 in DPYSL2-overexpressing cells to determine if EMT promotion depends on the DPYSL2-PKM2 interaction

  • Research has shown that PKM2 knockdown can block DPYSL2-induced enhancement of EMT in bladder cancer cells

These methodologies have demonstrated that DPYSL2 promotes EMT in bladder cancer via its interaction with PKM2, supporting tumor progression and metastasis .

What are the recommended approaches for developing and validating DPYSL2 as a therapeutic target?

Developing DPYSL2 as a therapeutic target requires systematic validation through multiple experimental approaches:

These approaches have supported DPYSL2 as a promising therapeutic target in both AML and bladder cancer, with potential applications in other cancer types as well .

How can researchers effectively compare and integrate DPYSL2 expression data across different cancer types?

Comparing DPYSL2 expression across cancer types requires careful methodology to ensure valid comparisons and meaningful integration:

• Data normalization and standardization:

  • Use appropriate housekeeping genes or global normalization methods when comparing qPCR data

  • Apply batch correction algorithms when integrating data from different sources

  • Normalize Western blot data to loading controls and reference standards

• Meta-analysis approaches:

  • Integrate data from public repositories (TCGA, GEO, GEPIA)

  • Apply statistical methods that account for inter-study heterogeneity

  • Use forest plots to visualize effect sizes across different cancer types

• Multi-omics integration:

  • Correlate DPYSL2 protein expression with mRNA levels

  • Integrate with methylation, mutation, and copy number variation data

  • Create comprehensive molecular profiles across cancer types

• Comparative analysis examples:

  • DPYSL2 is overexpressed in both AML and bladder cancer compared to normal tissues

  • High DPYSL2 expression correlates with poor prognosis in both cancer types, suggesting a conserved role in cancer progression

  • Different mechanisms may be involved: JAK2/STAT3/STAT5-PI3K P85/AKT/GSK3b in AML vs. PKM2 interaction in bladder cancer

• Visualization and analysis tools:

  • Use heatmaps to display expression patterns across cancer types

  • Employ principal component analysis to identify cancer clusters based on DPYSL2 and related gene expression

  • Create Kaplan-Meier plots to compare prognostic impact across different cancers

This integrative approach has revealed that while DPYSL2 may have conserved oncogenic functions across cancer types, the specific molecular mechanisms may differ, requiring cancer-specific therapeutic strategies .

What are the special considerations for using DPYSL2 antibodies in phosphorylation studies?

DPYSL2 undergoes extensive phosphorylation that regulates its function. When studying these modifications, researchers should consider:

• Phospho-specific antibody selection:

  • Choose antibodies that specifically recognize phosphorylated forms of DPYSL2 at key residues

  • Validate specificity using phosphatase treatment controls

  • Consider using multiple phospho-specific antibodies to study different phosphorylation sites simultaneously

• Sample preparation:

  • Include phosphatase inhibitors (sodium orthovanadate, sodium fluoride, β-glycerophosphate) in lysis buffers

  • Harvest samples quickly to preserve phosphorylation status

  • Consider using phospho-enrichment techniques for low-abundance phosphorylated forms

• Experimental design:

  • Include positive controls (samples treated with phosphatase inhibitors) and negative controls (samples treated with phosphatases)

  • Use phos-tag gels to separate phosphorylated from non-phosphorylated forms

  • Consider kinase inhibitor treatments to identify responsible kinases

• Interpretation challenges:

  • Phosphorylation can change rapidly in response to experimental conditions

  • Multiple phosphorylation sites may have different functional effects

  • Temporal dynamics of phosphorylation may be critical

• Relevance to disease mechanisms:

  • Altered phosphorylation of DPYSL2 may contribute to its role in the JAK2/STAT3/STAT5-PI3K P85/AKT/GSK3b signaling pathway in AML

  • Phosphorylation status may affect DPYSL2's interaction with proteins like PKM2 in cancer cells

These considerations ensure accurate detection and interpretation of DPYSL2 phosphorylation in both normal and pathological contexts.

How can researchers effectively use DPYSL2 antibodies in multiplex imaging studies?

Multiplex imaging allows simultaneous visualization of multiple proteins, providing valuable insights into complex cellular processes involving DPYSL2. Key methodological considerations include:

• Antibody selection for multiplexing:

  • Choose DPYSL2 antibodies from different host species than other target antibodies

  • Validate each antibody individually before multiplexing

  • Ensure specificity through appropriate controls

  • Select antibodies with compatible fixation and antigen retrieval requirements

• Sequential immunostaining approaches:

  • Perform cyclic immunofluorescence with antibody stripping between rounds

  • Use tyramide signal amplification (TSA) to allow use of antibodies from the same species

  • Document complete antibody removal between cycles

• Spectral considerations:

  • Select fluorophores with minimal spectral overlap

  • Use spectral unmixing for fluorophores with partial overlap

  • Include single-stain controls for accurate spectral separation

• Quantitative analysis:

  • Use image analysis software for co-localization quantification

  • Perform spatial relationship analysis between DPYSL2 and interacting partners

  • Consider using algorithms for cell phenotyping based on multiple markers

• Applications in DPYSL2 research:

  • Visualize DPYSL2 interaction with PKM2 in cancer cells

  • Study co-localization with components of the JAK2/STAT3/STAT5-PI3K pathway in AML

  • Examine spatial relationships between DPYSL2 and EMT markers in tumor tissue

These approaches allow researchers to study DPYSL2 in its native cellular context while preserving spatial information and relationships with other proteins of interest.

What are the optimal protocols for using DPYSL2 antibodies in flow cytometry?

While DPYSL2 is primarily a cytoplasmic protein, flow cytometry can be valuable for studying its expression in different cell populations. The following protocol optimizations are recommended:

• Cell preparation:

  • Fix cells with 4% paraformaldehyde for 15 minutes at room temperature

  • Permeabilize with 0.1% saponin or 0.1% Triton X-100 to access intracellular DPYSL2

  • Block with 3-5% BSA or normal serum for 30 minutes

• Antibody selection and staining:

  • Choose antibodies validated for flow cytometry applications

  • Titrate antibody concentration to determine optimal signal-to-noise ratio

  • Include isotype controls at the same concentration as the primary antibody

  • For multicolor panels, include fluorescence minus one (FMO) controls

• Protocol specifics:

  • Incubate with primary DPYSL2 antibody for 30-60 minutes at room temperature

  • Wash 2-3 times with buffer containing 0.1% saponin to maintain permeabilization

  • Incubate with fluorophore-conjugated secondary antibody for 30 minutes

  • Wash thoroughly before analysis

• Analysis considerations:

  • Gate on single, viable cells

  • Compare DPYSL2 expression levels between experimental groups

  • For cell differentiation analysis, co-stain with lineage markers like CD11b and CD14

• Applications in DPYSL2 research:

  • Quantify DPYSL2 expression changes following drug treatment

  • Assess infection efficiency in DPYSL2 knockdown experiments using GFP-labeled virus

  • Study DPYSL2 expression in different cell populations within heterogeneous samples

This approach enables quantitative assessment of DPYSL2 protein levels at the single-cell level, providing insights into expression heterogeneity within cell populations.

What emerging roles of DPYSL2 should researchers be exploring beyond its canonical functions?

Recent research has revealed several non-canonical functions of DPYSL2 that merit further investigation:

• Metabolic regulation:

  • DPYSL2's interaction with PKM2 and its role in promoting aerobic glycolysis in cancer cells represents a significant departure from its traditionally understood neuronal functions

  • Researchers should investigate whether DPYSL2 interacts with other metabolic enzymes beyond PKM2

  • The metabolic impact of DPYSL2 in non-cancer contexts remains largely unexplored

• Cancer progression mechanisms:

  • DPYSL2's role in promoting EMT suggests involvement in cancer metastasis beyond its metabolic functions

  • The mechanisms by which DPYSL2 promotes cell survival in cancer contexts need further exploration

  • The relationship between DPYSL2 and the tumor microenvironment remains poorly understood

• Drug resistance pathways:

  • DPYSL2's role in HHT resistance in AML suggests potential involvement in drug resistance mechanisms

  • Researchers should investigate whether DPYSL2 contributes to resistance to other therapeutic agents

  • The structural basis for HHT-DPYSL2 interaction provides a starting point for developing targeted inhibitors

• Signaling pathway integration:

  • The JAK2/STAT3/STAT5-PI3K P85/AKT/GSK3b pathway in AML and PKM2 interaction in bladder cancer suggest that DPYSL2 may integrate multiple signaling pathways

  • Comprehensive interactome studies could reveal additional signaling roles

• Therapeutic target development:

  • Structure-based drug design targeting the DPYSL2-PKM2 interaction or the HHT binding site could yield novel therapeutic approaches

  • DPYSL2 antibody-drug conjugates represent an unexplored therapeutic strategy

These emerging roles suggest that DPYSL2 functions extend well beyond its canonical role in neuronal development and axon guidance, opening new avenues for therapeutic intervention.

How might advanced technologies enhance DPYSL2 antibody applications in research?

Emerging technologies are expanding the capabilities of antibody-based research for DPYSL2 studies:

• Super-resolution microscopy techniques:

  • STORM, PALM, and STED microscopy can resolve DPYSL2 localization with nanometer precision

  • These techniques can reveal previously undetectable co-localization with interaction partners

  • Apply to studying DPYSL2-PKM2 interactions at the subcellular level

• Single-cell proteomics:

  • Mass cytometry (CyTOF) can simultaneously measure DPYSL2 and dozens of other proteins at the single-cell level

  • Single-cell Western blot technology allows protein analysis in individual cells

  • These approaches can reveal heterogeneity in DPYSL2 expression and modification within cell populations

• Spatial transcriptomics and proteomics:

  • Combine DPYSL2 antibody staining with spatial transcriptomics to correlate protein localization with gene expression

  • Digital spatial profiling can map DPYSL2 distribution in tissue contexts with high precision

  • These technologies are particularly valuable for studying DPYSL2 in tumor microenvironments

• Proximity-based labeling:

  • BioID or APEX2 fused to DPYSL2 can identify proximal proteins in living cells

  • These techniques can reveal transient or weak interactions missed by traditional co-IP

  • Apply to discovering novel DPYSL2 interaction partners beyond PKM2

• High-throughput screening platforms:

  • Antibody arrays and reverse phase protein arrays enable rapid profiling of DPYSL2 across multiple samples

  • CRISPR screens combined with DPYSL2 antibody detection can identify genes affecting DPYSL2 expression or function

  • These approaches accelerate discovery of pathways regulating DPYSL2 in disease contexts

These advanced technologies promise to deepen our understanding of DPYSL2's roles in normal physiology and disease, potentially leading to novel therapeutic strategies.

How can researchers integrate multi-omics data with DPYSL2 antibody-based experiments?

Integrating multi-omics data with antibody-based experiments provides a comprehensive understanding of DPYSL2 biology:

• Correlative analysis approaches:

  • Compare DPYSL2 protein levels (detected by antibodies) with mRNA expression (from RNA-seq)

  • Correlate post-translational modifications with proteomic datasets

  • Integrate epigenetic data to understand regulatory mechanisms of DPYSL2 expression

• Network analysis:

  • Place DPYSL2 in protein-protein interaction networks using antibody-based interaction studies

  • Overlay transcriptomic data to identify co-expressed genes

  • Identify regulatory modules controlling DPYSL2 expression and function

• Methodological approaches:

  • Use DPYSL2 antibodies for ChIP-seq to identify genomic binding sites (if DPYSL2 has DNA-binding capacity)

  • Combine proteomics with DPYSL2 immunoprecipitation to identify interaction partners

  • Validate RNA-seq findings with protein-level measurements using DPYSL2 antibodies

• Applications in cancer research:

  • RNA-seq analysis from TCGA database combined with immunohistochemistry has revealed the JAK2/STAT3/STAT5-PI3K P85/AKT/GSK3b axis as a critical pathway in DPYSL2-mediated AML development

  • Integration of proteomic and metabolomic data with DPYSL2 antibody studies has helped elucidate its role in regulating PKM2 and aerobic glycolysis in bladder cancer

• Data visualization and analysis tools:

  • Use pathway analysis software to integrate antibody-based protein data with transcriptomic findings

  • Employ machine learning approaches to identify patterns across multi-omics datasets

  • Create integrative visualizations that connect DPYSL2 protein expression with other molecular features

This integrative approach provides a systems-level understanding of DPYSL2's role in health and disease, enabling more effective therapeutic targeting strategies.