GPR137 Antibody

What is GPR137 and why is it significant in research?

GPR137 (G protein-coupled receptor 137) is a member of the G protein-coupled receptor superfamily that was initially reported as a novel orphan GPR approximately a decade ago. The significance of GPR137 lies in its ubiquitous expression in the central nervous system (CNS), primarily in the hippocampus, and its emerging role as a potential oncogene in various cancers. Research has demonstrated that GPR137 is involved in the progression of human glioma, suggesting its potential oncogenic role in glioma cells. Additionally, recent studies have highlighted GPR137's important function in colon cancer cell proliferation and its role in gastric cancer through Hippo signaling pathway modulation . The increasing evidence of GPR137's involvement in multiple cancer types makes it a promising target for both diagnostic and therapeutic applications, necessitating reliable antibodies for its detection and characterization.

What applications are GPR137 antibodies validated for?

GPR137 antibodies have been validated for multiple research applications, making them versatile tools for investigating this protein. According to the available data, the antibody has been tested and validated for the following applications:

For immunohistochemistry applications, positive detection has been reported in mouse brain tissue and human gliomas tissue. Technical notes suggest antigen retrieval with TE buffer pH 9.0, though citrate buffer pH 6.0 may serve as an alternative . It is strongly recommended to optimize antibody dilutions for each specific experimental system to obtain optimal results, as sensitivity can be sample-dependent.

What are the optimal storage conditions for GPR137 antibodies?

Proper storage of antibodies is crucial for maintaining their efficacy and specificity. For GPR137 antibodies, the optimal storage conditions depend on the specific formulation. For standard preparations containing preservatives (PBS with 0.02% sodium azide and 50% glycerol, pH 7.3), storage at -20°C is recommended, where the antibody remains stable for one year after shipment. For these preparations, aliquoting is unnecessary for -20°C storage . For specialized formulations containing only PBS without preservatives, more stringent storage at -80°C is recommended to maintain antibody integrity . It is essential to avoid repeated freeze-thaw cycles as they can denature antibodies and reduce their performance. When working with smaller quantities (20μl sizes), it's important to note that some preparations may contain 0.1% BSA as a stabilizer . Always refer to the specific product documentation as storage recommendations may vary between manufacturers and formulations.

What is the reactivity profile of GPR137 antibodies?

The reactivity profile of GPR137 antibodies indicates which species' samples the antibody can effectively detect. Based on the search results, GPR137 antibodies (such as 11929-1-AP) have been tested and confirmed to react with human, mouse, and rat samples . This cross-species reactivity is particularly valuable for comparative studies and translational research. While the antibody has been experimentally validated in these three species, additional species may share sufficient homology in the antibody's epitope region to allow cross-reactivity. The antibody was raised against a GPR137 fusion protein (Ag2611), and prediction algorithms may suggest additional potential reactive species based on sequence conservation analysis . For researchers working with species not explicitly listed in the validated reactivity profile, preliminary validation experiments are strongly recommended before proceeding with full-scale studies.

What is the role of GPR137 in the Hippo signaling pathway in gastric cancer progression?

Recent research has uncovered a significant mechanistic relationship between GPR137 and the Hippo signaling pathway in gastric cancer progression. GPR137 expression is notably upregulated in gastric cancer tissues compared to adjacent normal tissues, as demonstrated by both the Gene Expression Profiling Interactive Analysis (GEPIA) database and immunohistochemistry validation. The mechanism involves GPR137 binding to MST kinases, which are upstream components of the Hippo pathway. This binding disrupts the association of MST with LATS, subsequently activating transcriptional co-activators YAP and TAZ .

The functional consequences of this GPR137-mediated Hippo pathway inactivation are profound. Overexpression of GPR137 significantly enhances multiple aspects of gastric cancer AGS cell malignancy, including:

• Increased cell proliferation in a time-dependent manner

• Accelerated gap closure in wound healing assays

• Enhanced cell invasion in matrigel-transwell assays

• Stimulated colony formation

• Increased xenograft tumor weight and volume in nude mice

Conversely, CRISPR/Cas9-mediated knockout of GPR137 produces opposite effects, reducing these malignant characteristics . This mechanistic relationship suggests that GPR137 could serve as a potential therapeutic target for gastric cancer, with antibodies against GPR137 being valuable tools for both research and potential clinical applications targeting this pathway.

How can researchers troubleshoot non-specific binding when using GPR137 antibodies in immunohistochemistry?

Non-specific binding is a common challenge when using antibodies in immunohistochemistry (IHC), and GPR137 antibodies are no exception. To troubleshoot this issue with GPR137 antibodies, researchers should implement a systematic approach:

• Optimize antigen retrieval conditions: For GPR137 antibodies, the suggested antigen retrieval method uses TE buffer at pH 9.0, though citrate buffer at pH 6.0 may serve as an alternative . Inadequate antigen retrieval can reduce specific binding while potentially maintaining non-specific interactions.

• Titrate antibody concentration: The recommended dilution range for GPR137 antibodies in IHC is 1:50-1:500 . Begin with a midrange dilution (e.g., 1:200) and adjust based on signal-to-noise ratio. Over-concentrated antibody solutions frequently produce high background.

• Extend blocking steps: Increase blocking time or use alternative blocking agents (e.g., 5% normal serum from the same species as the secondary antibody) to reduce non-specific binding.

• Include additional washing steps: After both primary and secondary antibody incubations, implement additional washing steps with PBS containing 0.1-0.3% Tween-20 to remove weakly bound antibodies.

• Validate with positive and negative controls: Include known GPR137-expressing tissues (such as mouse brain tissue or human gliomas) as positive controls , and use either GPR137-knockout tissues or primary antibody omission as negative controls.

• Consider tissue-specific autofluorescence: When performing IF with GPR137 antibodies, treat sections with autofluorescence quenching agents appropriate for the tissue being examined.

• Validate specificity with peptide competition: Pre-incubate the GPR137 antibody with the immunizing peptide before application to verify that the observed staining is specific to GPR137.

These methodological adjustments should significantly improve specificity when using GPR137 antibodies for IHC applications.

How does GPR137 expression vary across different cancer types, and what are the implications for using GPR137 antibodies in cancer research?

GPR137 exhibits differential expression patterns across various cancer types, which has significant implications for cancer research utilizing GPR137 antibodies. Based on current research findings:

• Gastric cancer: GPR137 is significantly upregulated in stomach adenocarcinoma (STAD) tissue compared to normal gastric tissue, as confirmed by both database analysis and immunohistochemistry staining . This upregulation correlates with increased malignancy.

• Glioma: GPR137 is involved in the progression of human glioma, suggesting its role as a potential oncogene in glioma cells .

• Colon cancer: Studies have demonstrated GPR137's important role in colon cancer cell proliferation .

• Other cancers: Evidence suggests GPR137 involvement in ovarian, pancreatic, hepatoma, bladder, and prostate cancers, as well as medulloblastoma .

These varying expression patterns have several implications for researchers:

• Antibody validation: When studying a specific cancer type, researchers should validate GPR137 antibody specificity in that particular tissue context, as different tissue microenvironments may affect epitope accessibility.

• Quantitative considerations: Different baseline expression levels may necessitate adjustments in antibody dilutions or detection methods between cancer types.

• Control selection: Appropriate normal tissue controls should be carefully selected based on the cancer type being studied.

• Prognostic potential: The correlation between GPR137 expression and malignancy suggests GPR137 antibodies could potentially serve as prognostic tools in multiple cancer types, though extensive validation would be required.

• Therapeutic targeting: The widespread involvement of GPR137 in various cancers suggests it could be a broad-spectrum therapeutic target, with antibodies serving as valuable research tools for mechanism elucidation.

Understanding these cancer-specific variations in GPR137 expression is essential for accurately interpreting research findings and developing targeted applications using GPR137 antibodies.

What considerations should be made when designing co-immunoprecipitation experiments to study GPR137 interactions with components of the Hippo pathway?

Co-immunoprecipitation (Co-IP) experiments to investigate GPR137 interactions with Hippo pathway components require careful consideration of several methodological aspects:

• Antibody selection: Choose GPR137 antibodies that have been validated for immunoprecipitation applications. The antibody should recognize the native, non-denatured form of GPR137. Consider using multiple antibodies targeting different epitopes to confirm results.

• Epitope accessibility: Since research indicates that GPR137 binds to MST kinases , ensure the chosen antibody's epitope does not overlap with or sterically hinder the GPR137-MST interaction surface. Ideally, use antibodies that target regions distinct from the predicted interaction domains.

• Cell lysis conditions: GPR137 is a transmembrane protein with multiple membrane-spanning domains. Use mild detergents (e.g., 1% NP-40 or 0.5% Triton X-100) that solubilize membrane proteins while preserving protein-protein interactions. Avoid harsh detergents like SDS that may disrupt the GPR137-MST interaction.

• Buffer optimization: Include protease and phosphatase inhibitors in all buffers to prevent degradation. For studying interactions with the Hippo pathway components (particularly kinases like MST), phosphatase inhibitors are crucial to maintain the phosphorylation state that may be essential for the interaction.

• Controls: Include critical controls such as:

  • IgG control from the same species as the GPR137 antibody

  • Input samples (pre-immunoprecipitation lysate)

  • Reverse Co-IP (immunoprecipitate with anti-MST antibody and detect GPR137)

  • Samples with GPR137 knockdown/knockout to confirm specificity

• Validation strategy: Confirm the GPR137-MST interaction using complementary approaches such as:

  • Proximity ligation assay (PLA)

  • Bioluminescence resonance energy transfer (BRET)

  • Fluorescence resonance energy transfer (FRET)

  • Mammalian two-hybrid assay

• Detection considerations: When performing western blot analysis of Co-IP samples, use antibodies from different species for immunoprecipitation and detection to avoid detecting the heavy and light chains of the immunoprecipitating antibody.

By carefully considering these methodological aspects, researchers can design robust Co-IP experiments to investigate the interaction between GPR137 and components of the Hippo pathway, potentially revealing new therapeutic targets in cancers where this interaction drives malignancy.

How can researchers quantitatively assess changes in GPR137 expression in response to experimental interventions?

Quantitative assessment of GPR137 expression changes requires rigorous methodological approaches. Researchers can employ multiple complementary techniques for comprehensive evaluation:

• Western Blot Analysis:

  • Use validated GPR137 antibodies with appropriate loading controls (β-actin, GAPDH, etc.)

  • Implement densitometric analysis using software such as ImageJ

  • Include standard curves of recombinant GPR137 for absolute quantification

  • Normalize GPR137 signal to loading controls and present as fold-change relative to baseline/control conditions

• Quantitative Real-Time PCR (qRT-PCR):

  • Design primers specific to GPR137 mRNA

  • Validate primer efficiency using standard curves

  • Apply the ΔΔCt method for relative quantification

  • Use multiple reference genes (GAPDH, β-actin, 18S rRNA) for normalization

  • Correlate mRNA changes with protein levels detected by antibodies to address potential post-transcriptional regulation

• Immunohistochemistry/Immunofluorescence Quantification:

  • Use GPR137 antibodies at optimized dilutions (1:50-1:500 for IHC)

  • Apply automated image analysis software (QuPath, ImageJ, etc.)

  • Implement H-score, Allred score, or mean fluorescence intensity (MFI) quantification

  • Analyze multiple fields per sample (minimum 5-10 fields)

  • Blind the analysis to experimental conditions

• Flow Cytometry:

  • Optimize GPR137 antibody staining protocols for permeabilized cells

  • Use median fluorescence intensity (MFI) for quantification

  • Include fluorescence-minus-one (FMO) controls

  • Compare results with other quantitative methods

• ELISA-Based Methods:

  • Develop sandwich ELISA using GPR137 antibodies

  • Generate standard curves using recombinant GPR137

  • Validate assay sensitivity and dynamic range

  • Ensure sample preparation maintains GPR137 antigenicity

• Statistical Considerations:

  • Perform power analysis to determine appropriate sample sizes

  • Apply appropriate statistical tests (t-test, ANOVA with post-hoc tests)

  • Report effect sizes alongside p-values

  • Confirm reproducibility across independent experiments

• Validation Approaches:

  • Compare expression changes using multiple GPR137 antibodies targeting different epitopes

  • Validate with genetic approaches (siRNA, CRISPR/Cas9) as controls

  • Consider temporal dynamics by assessing expression at multiple time points

By integrating multiple quantitative approaches, researchers can robustly assess changes in GPR137 expression while minimizing technique-specific biases and artifacts.

What are the optimal antigen retrieval protocols for GPR137 immunohistochemistry in different tissue types?

Antigen retrieval is a critical step in immunohistochemistry that significantly impacts the sensitivity and specificity of GPR137 detection. Based on available data, the following tissue-specific protocols are recommended:

For brain tissue and gliomas:

• Primary recommendation: Heat-induced epitope retrieval (HIER) using TE buffer at pH 9.0

• Alternative approach: HIER using citrate buffer at pH 6.0

The optimal protocol may vary based on tissue type, fixation conditions, and embedding methods. For standardization and optimization in specific tissue contexts:

• Tissue-specific considerations:

  • Highly fixated tissues (e.g., archived FFPE samples): Extend retrieval time by 5-10 minutes beyond standard protocols

  • Lipid-rich tissues (e.g., brain): Include 0.1% Tween-20 in retrieval buffer to enhance penetration

  • Gastric tissue: Pre-treatment with 0.05% pepsin (10 minutes at 37°C) before HIER may improve epitope accessibility

• Method optimization:

  • Temperature and duration: Begin with 95-98°C for 20 minutes; adjust in 5-minute increments if necessary

  • Pressure considerations: Pressure cooker methods (110°C, 3-5 minutes) may provide superior results for certain tissue types

  • Cooling period: Allow gradual cooling (20-30 minutes) to room temperature before proceeding with blocking

• Validation approach:

  • Test multiple retrieval conditions side-by-side

  • Evaluate signal intensity, background levels, and morphological preservation

  • Include positive control tissues (mouse brain or human gliomas for GPR137)

  • Document optimal conditions for each tissue type and fixation method

• Troubleshooting guidance:

  • Weak signal: Extend retrieval time or increase temperature

  • High background: Reduce retrieval time or temperature; add additional blocking steps

  • Tissue detachment: Apply tissue adhesive slides or reduce retrieval aggressiveness

By systematically optimizing antigen retrieval protocols for specific tissue types, researchers can maximize the sensitivity and specificity of GPR137 detection while preserving tissue morphology and minimizing artifacts.

What controls should be included when validating GPR137 antibody specificity in new experimental systems?

Rigorous validation of GPR137 antibody specificity requires a comprehensive set of controls when implementing in new experimental systems:

• Positive tissue controls:

  • Mouse brain tissue (particularly hippocampus) - known to express GPR137

  • Human gliomas tissue - confirmed to express GPR137

  • Gastric cancer tissue - shown to have upregulated GPR137 expression

• Negative controls:

  • Primary antibody omission: Replace primary antibody with antibody diluent

  • Isotype control: Use non-specific IgG from the same host species (rabbit for most GPR137 antibodies)

  • Pre-absorption control: Pre-incubate antibody with immunizing peptide/protein

  • Genetically modified samples: Use CRISPR/Cas9 GPR137 knockout cells/tissues as definitive negative controls

• Orthogonal validation:

  • Multiple antibodies: Test different GPR137 antibodies targeting distinct epitopes

  • Correlation with mRNA: Parallel assessment of GPR137 mRNA levels via qPCR or in situ hybridization

  • Tagged protein: Compare with exogenously expressed tagged GPR137 (e.g., FLAG, HA, GFP)

• Knockdown/overexpression validation:

  • siRNA/shRNA knockdown: Confirm reduced signal with GPR137 knockdown

  • Overexpression: Validate increased signal with GPR137 overexpression

  • Dose-response relationship: Demonstrate proportional signal changes with varying expression levels

• Western blot validation:

  • Confirm single band at expected molecular weight (calculated as 44 kDa)

  • Run alongside molecular weight markers

  • Include known positive and negative control lysates

• Cross-reactivity assessment:

  • Test antibody performance in multiple species (human, mouse, rat)

  • Evaluate potential cross-reactivity with closely related proteins (e.g., other GPR family members)

• Reproducibility verification:

  • Test antibody across multiple biological replicates

  • Evaluate lot-to-lot consistency if using the same antibody from different batches

By systematically implementing these controls, researchers can confidently validate GPR137 antibody specificity in new experimental systems, ensuring reliable and reproducible results.

How can researchers design effective experimental protocols to investigate GPR137's role in cancer progression using antibody-based techniques?

Designing effective experimental protocols to investigate GPR137's role in cancer progression requires a multifaceted approach that leverages antibody-based techniques across various dimensions of cancer biology:

• Expression profiling across cancer stages:

  • Use GPR137 antibodies for IHC analysis of tissue microarrays containing samples from different cancer stages

  • Apply standardized scoring systems (H-score, Allred, etc.) for quantification

  • Correlate expression with clinicopathological parameters and patient outcomes

  • Compare with matched normal tissues to establish baseline expression

• Functional studies in cancer cell models:

  • Knockdown/knockout approaches:

    • Generate GPR137 knockdown (siRNA/shRNA) or knockout (CRISPR/Cas9) cancer cell lines

    • Validate altered expression using GPR137 antibodies in Western blot and IF

    • Assess effects on proliferation, migration, invasion, and colony formation

    • Evaluate xenograft growth in vivo

  • Overexpression approaches:

    • Create stable GPR137-overexpressing cancer cell lines

    • Confirm overexpression using GPR137 antibodies

    • Assess functional outcomes in parallel with knockdown models

• Signaling pathway analysis:

  • Hippo pathway investigation:

    • Use co-immunoprecipitation with GPR137 antibodies to identify interactions with MST kinases

    • Assess phosphorylation status of pathway components (YAP/TAZ) following GPR137 manipulation

    • Perform nuclear/cytoplasmic fractionation to track YAP/TAZ localization using antibodies

    • Conduct ChIP assays to assess YAP/TAZ binding to target promoters

  • Other potential pathways:

    • Investigate GPCR-typical pathways (G-protein activation, cAMP, Ca²⁺ signaling)

    • Screen for phosphorylation changes in key oncogenic pathways using phospho-specific antibodies

• Mechanistic dissection:

  • Protein-protein interaction mapping:

    • Perform systematic co-immunoprecipitation with GPR137 antibodies followed by mass spectrometry

    • Validate key interactions with reciprocal co-IP

    • Use proximity ligation assay (PLA) to confirm interactions in situ

  • Functional domain analysis:

    • Generate truncated or mutated GPR137 constructs

    • Use domain-specific antibodies to assess expression and localization

    • Determine which domains are critical for cancer-promoting functions

• Therapeutic potential assessment:

  • Antibody-mediated targeting:

    • Evaluate effects of GPR137-neutralizing antibodies on cancer cell phenotypes

    • Test combinations with established cancer therapies

    • Assess potential for antibody-drug conjugate development

  • Small molecule screening:

    • Use GPR137 antibodies to validate target engagement of candidate molecules

    • Confirm mechanism of action through pathway analysis

• Clinical correlation studies:

  • Patient-derived samples:

    • Apply GPR137 antibodies to patient-derived xenografts or organoids

    • Correlate expression with treatment response

    • Evaluate potential as a predictive biomarker

By systematically implementing these experimental approaches using validated GPR137 antibodies, researchers can comprehensively investigate GPR137's role in cancer progression and evaluate its potential as a therapeutic target.

How can researchers reconcile contradictory findings when using different GPR137 antibodies across experimental systems?

Contradictory findings when using different GPR137 antibodies present a significant challenge in research. A systematic approach to reconcile such discrepancies includes:

• Epitope mapping analysis:

  • Determine the precise epitopes recognized by each antibody

  • Assess whether antibodies target different domains of GPR137

  • Consider that transmembrane proteins like GPR137 may present different epitopes depending on conformation

  • Evaluate epitope conservation across species for cross-reactivity issues

• Antibody validation comparison:

  • Review validation data for each antibody (Western blot, IHC, IF)

  • Assess specificity using knockout/knockdown controls

  • Compare lot-to-lot consistency within the same antibody product

  • Evaluate polyclonal versus monoclonal antibody characteristics

• Protocol standardization:

  • Implement identical experimental conditions when comparing antibodies

    • Use the same antigen retrieval methods for IHC

    • Apply consistent blocking and washing procedures

    • Standardize fixation protocols

  • Test antibodies side-by-side in controlled experiments

• Context-dependent expression assessment:

  • Consider that GPR137 expression may be genuinely different across:

    • Cell/tissue types (e.g., brain versus gastric tissue)

    • Disease states (normal versus cancer)

    • Experimental manipulations (treatment conditions)

  • Use orthogonal methods (qPCR, mass spectrometry) to validate expression patterns

• Post-translational modification analysis:

  • Investigate whether GPR137 undergoes modifications that affect antibody recognition

  • Consider phosphorylation, glycosylation, or proteolytic processing

  • Use phosphatase or glycosidase treatments to assess impact on antibody binding

• Isoform consideration:

  • Determine whether different antibodies recognize distinct GPR137 isoforms

  • Analyze alternative splicing patterns in different tissues/conditions

  • Design isoform-specific detection strategies

• Quantitative correlation analysis:

  • Plot results from different antibodies to identify systematic biases

  • Establish correction factors if consistent patterns emerge

  • Determine whether discrepancies are quantitative or qualitative

• Collaborative validation:

  • Engage with other laboratories to independently test antibodies

  • Implement ring trials with standardized protocols

  • Share raw data and analysis methods for transparent comparison

When reporting findings, researchers should transparently document which antibody was used, acknowledge potential limitations, and discuss how contradictory findings were addressed. This approach builds confidence in results and advances the field's understanding of GPR137 biology.

What are the challenges in correlating GPR137 expression with clinical outcomes in cancer patients?

Correlating GPR137 expression with clinical outcomes in cancer patients presents several methodological and interpretative challenges that researchers must address:

• Tissue heterogeneity considerations:

  • Intratumoral heterogeneity may lead to sampling bias

  • GPR137 expression may vary across different regions of the same tumor

  • Implementation strategies:

    • Use multiple tumor cores from different regions in tissue microarrays

    • Apply digital pathology with whole-slide imaging to assess spatial distribution

    • Consider single-cell approaches to resolve cell-type specific expression

• Analytical standardization challenges:

  • Lack of standardized scoring systems for GPR137 immunohistochemistry

  • Variability in antibody performance across laboratories

  • Implementation strategies:

    • Establish consensus cutoff values for "high" versus "low" expression

    • Implement automated image analysis to reduce observer bias

    • Use continuous expression metrics rather than binary classifications

• Multivariate analysis complexity:

  • GPR137 expression may interact with other molecular markers

  • Confounding clinical variables may mask true correlations

  • Implementation strategies:

    • Apply robust multivariate models adjusting for known prognostic factors

    • Include molecular subtypes in stratification

    • Consider machine learning approaches for complex pattern recognition

• Temporal dynamics considerations:

  • GPR137 expression may change during disease progression

  • Treatment may alter expression patterns

  • Implementation strategies:

    • Analyze matched samples from diagnosis, during treatment, and at progression

    • Perform longitudinal blood-based testing where feasible

    • Correlate expression changes with treatment response

• Functional relevance assessment:

  • Expression alone may not reflect functional activity

  • Potential disconnect between mRNA and protein levels

  • Implementation strategies:

    • Assess phosphorylation status of downstream targets (e.g., Hippo pathway components)

    • Combine with functional assays in patient-derived models

    • Integrate with other 'omics data for pathway activity inference

• Cancer-type specificity challenges:

  • GPR137's prognostic significance likely varies across cancer types

  • Differential pathway activation in different cancers

  • Implementation strategies:

    • Perform cancer-type specific analyses

    • Consider pan-cancer studies to identify common patterns

    • Validate findings across independent cohorts within the same cancer type

• Translational barriers:

  • Moving from retrospective correlation to prospective clinical utility

  • Analytical validation of GPR137 as a biomarker

  • Implementation strategies:

    • Design prospective studies with pre-specified endpoints

    • Develop standardized clinical assays with quality control

    • Validate in multi-institutional settings

By systematically addressing these challenges, researchers can establish more reliable correlations between GPR137 expression and clinical outcomes, potentially advancing this marker toward clinical utility in cancer management.

What emerging technologies might enhance GPR137 antibody applications in cancer research?

Several cutting-edge technologies are poised to revolutionize GPR137 antibody applications in cancer research:

• Spatial transcriptomics integration:

  • Combine GPR137 antibody-based immunohistochemistry with spatial transcriptomics

  • Map GPR137 protein expression in relation to transcriptional signatures

  • Identify spatial relationships between GPR137-expressing cells and their microenvironment

  • Potential to reveal functional niches within tumors where GPR137 signaling is most active

• Mass cytometry (CyTOF) and imaging mass cytometry:

  • Incorporate metal-conjugated GPR137 antibodies into multi-parameter panels

  • Simultaneously assess up to 40 proteins including GPR137 and Hippo pathway components

  • Generate high-dimensional single-cell data to identify novel cell populations

  • Spatial mapping of GPR137 in relation to multiple markers in tissue sections

• Super-resolution microscopy approaches:

  • Apply techniques like STORM, PALM, or STED using fluorophore-conjugated GPR137 antibodies

  • Achieve nanoscale resolution of GPR137 localization

  • Study co-localization with interaction partners (e.g., MST kinases)

  • Investigate dynamic changes in GPR137 distribution during signaling events

• Proximity-based proteomics:

  • Implement BioID or APEX2 proximity labeling fused to GPR137

  • Identify novel proximal proteins in living cells

  • Validate interactions using co-immunoprecipitation with GPR137 antibodies

  • Map the dynamic "interactome" of GPR137 in different cancer contexts

• Single-cell proteomics:

  • Apply single-cell Western blot or microfluidic antibody-based platforms

  • Assess GPR137 expression heterogeneity at single-cell resolution

  • Correlate with functional phenotypes and other protein markers

  • Identify rare cell populations with distinct GPR137 expression patterns

• Antibody-enabled liquid biopsy approaches:

  • Develop sensitive assays for detecting GPR137 or GPR137-expressing extracellular vesicles in blood

  • Use antibody-based capture of circulating tumor cells expressing GPR137

  • Monitor GPR137 expression dynamics during treatment

  • Enable longitudinal non-invasive assessment of GPR137 status

• Antibody-drug conjugates (ADCs) and therapeutic development:

  • Engineer GPR137 antibodies as delivery vehicles for cytotoxic payloads

  • Evaluate internalization kinetics and intracellular trafficking

  • Assess potential for targeted therapy in GPR137-overexpressing cancers

  • Combine with Hippo pathway inhibitors for synergistic effects

• Theranostic applications:

  • Develop dual-purpose GPR137 antibodies for both imaging and therapy

  • Conjugate with radioisotopes for PET/SPECT imaging and radiotherapy

  • Enable patient selection and treatment monitoring

  • Create personalized treatment approaches based on GPR137 expression

By leveraging these emerging technologies, researchers can significantly enhance the utility of GPR137 antibodies in cancer research, potentially accelerating the translation of basic findings into clinical applications.

How might GPR137 antibodies contribute to understanding the role of this receptor in neurological disorders, given its expression in the hippocampus?

Given GPR137's ubiquitous expression in the central nervous system, particularly in the hippocampus , GPR137 antibodies could make significant contributions to understanding its role in neurological disorders through several research avenues:

• Spatial-temporal expression mapping:

  • Use GPR137 antibodies to create high-resolution expression maps across brain regions

  • Track developmental expression patterns from embryonic to adult stages

  • Compare expression in normal versus pathological conditions

  • Implement cell-type specific co-localization with neuronal, glial, and vascular markers

• Hippocampal function investigation:

  • Examine GPR137 distribution across hippocampal subfields (CA1-CA4, dentate gyrus)

  • Correlate with functional domains involved in memory formation and spatial navigation

  • Assess activity-dependent changes in GPR137 expression

  • Investigate potential roles in adult neurogenesis within the dentate gyrus

• Neurodegenerative disease applications:

  • Analyze GPR137 expression in Alzheimer's disease models and patient samples

  • Investigate potential alterations in Parkinson's disease and other neurodegenerative conditions

  • Assess relationships with disease-associated proteins (Aβ, tau, α-synuclein)

  • Evaluate as a potential biomarker for disease progression

• Neuroinflammatory context:

  • Examine GPR137 expression in microglia and astrocytes during inflammatory responses

  • Investigate changes in expression following acute injury or chronic inflammation

  • Assess potential roles in blood-brain barrier function

  • Evaluate as a target for modulating neuroinflammation

• Synaptic plasticity studies:

  • Use super-resolution microscopy with GPR137 antibodies to localize the receptor at synapses

  • Investigate changes in expression during long-term potentiation or depression

  • Assess relationship with synaptic proteins and receptors

  • Evaluate potential roles in synaptic scaling and homeostasis

• Circuit-level analyses:

  • Combine GPR137 antibody staining with circuit tracing techniques

  • Identify specific neuronal populations and projections expressing GPR137

  • Correlate with electrophysiological properties

  • Implement cell-type specific manipulations to assess functional consequences

• Therapeutic target evaluation:

  • Screen for compounds that modulate GPR137 function

  • Use antibodies to validate target engagement in brain tissue

  • Develop neurological disease models based on GPR137 dysfunction

  • Assess potential for antibody-based therapeutics in neurological conditions

• Translational applications:

  • Develop GPR137 antibody-based assays for cerebrospinal fluid

  • Evaluate as a diagnostic or prognostic marker in neurological disorders

  • Implement in patient stratification for clinical trials

  • Explore imaging applications with engineered antibody fragments

By systematically applying these approaches, researchers can leverage GPR137 antibodies to elucidate the receptor's roles in normal brain function and neurological disorders, potentially opening new avenues for therapeutic intervention beyond the current focus on cancer.