SLC35C1 Antibody

What is SLC35C1 and why is it significant in biomedical research?

SLC35C1, also known as GDP-fucose transporter 1, CDG2C, or FUCT1, belongs to the solute carrier (SLC) protein group. It was first identified in leucocyte adhesion deficiency II (LAD II) patients who exhibited reduced GDP-fucose transport into the Golgi apparatus . The protein primarily localizes to secretion-related subcellular structures, including the Golgi apparatus, endoplasmic reticulum (ER), and early and late endosomes, as confirmed by immunofluorescence studies . SLC35C1's significance stems from its essential role in fucosylation processes and its newly discovered function as a negative regulator of the canonical Wnt signaling pathway, which is critically involved in cell proliferation and cancer development, particularly in colorectal carcinogenesis .

How does SLC35C1 distribution vary across cellular compartments and tissues?

SLC35C1 exhibits specific subcellular localization patterns that reflect its function in fucosylation. Immunofluorescence studies have confirmed that SLC35C1 primarily colocalizes with the Golgi apparatus marker protein GM130 in HEK293 cells, supporting its well-established role in Golgi-mediated fucosylation . Additionally, SLC35C1 has been detected in association with calnexin (an ER marker), as well as Rab5 and Rab7 (markers for early and late endosomes, respectively) . Notably, SLC35C1 is absent from lysosomes (labeled by Lamp1) and mitochondria (labeled by TOM20) . In tissue distribution studies, SLC35C1 expression shows significant variance between normal and cancerous tissues, with marked downregulation observed in colon cancer tissues across all stages .

What are the recommended controls when using SLC35C1 antibodies in experimental procedures?

When using SLC35C1 antibodies, several controls are essential for experimental validation:

• Positive tissue controls: Normal colon tissue samples exhibit higher SLC35C1 expression compared to cancerous tissues and can serve as positive controls .

• Negative controls: SLC35C1-silenced cell lines (using shRNA or CRISPR-Cas9 systems) provide excellent negative controls .

• Subcellular localization controls: Co-staining with established markers such as GM130 (Golgi), calnexin (ER), Rab5 (early endosomes), and Rab7 (late endosomes) helps confirm specific subcellular localization .

• Expression validation: Western blot analysis following SLC35C1 silencing or overexpression confirms antibody specificity .

• Cross-reactivity assessment: Testing in multiple cell lines helps establish the consistency of SLC35C1 detection across different cellular backgrounds.

What are the optimal immunohistochemistry protocols for SLC35C1 detection in tissue samples?

For optimal immunohistochemical detection of SLC35C1 in tissue samples, researchers should follow these methodological guidelines:

• Tissue preparation: Formalin-fixed, paraffin-embedded tissues should be sectioned at 4-5 μm thickness.

• Antigen retrieval: Heat-mediated antigen retrieval in citrate buffer (pH 6.0) is recommended.

• Blocking: Use 5% normal goat serum in PBS with 0.1% Triton X-100 for 1 hour at room temperature.

• Primary antibody: Apply SLC35C1 rabbit polyclonal antibody (such as Abcam #ab60336) at 1:100-1:200 dilution and incubate overnight at 4°C .

• Secondary antibody: Use peroxidase AffiniPure Goat Anti-Rabbit IgG (such as Jackson ImmunoResearch #111-035-144) at 1:500 dilution for 1 hour at room temperature .

• Visualization: Develop with DAB substrate and counterstain with hematoxylin.

• Controls: Include both positive (normal colon tissue) and negative (primary antibody omitted) controls in each experiment.

This protocol has been successfully employed to demonstrate differential expression of SLC35C1 between normal and cancerous colon tissues .

How can researchers effectively perform co-localization studies with SLC35C1 antibodies?

To perform effective co-localization studies using SLC35C1 antibodies, researchers should implement the following methodological approach:

• Cell preparation: Culture cells on glass coverslips and fix with 4% paraformaldehyde for 15 minutes at room temperature.

• Permeabilization: Treat with 0.1% Triton X-100 in PBS for 10 minutes.

• Blocking: Apply 5% BSA in PBS for 30 minutes.

• Primary antibodies: Co-incubate with SLC35C1 rabbit polyclonal antibody (1:200) and organelle marker antibodies such as:

  • GM130 for Golgi apparatus

  • Calnexin for ER (Cell Signaling #2679)

  • Rab5 for early endosomes (Cell Signaling #3547)

  • Rab7 for late endosomes (Cell Signaling #9367)

• Secondary antibodies: Apply species-specific fluorescent-conjugated antibodies, such as:

  • Goat anti-rabbit-Cy2 (Jackson ImmunoResearch #111-225-144)

  • Goat anti-mouse-Cy3 (Jackson ImmunoResearch #115-165-146)

• Imaging: Use confocal microscopy with appropriate filter sets to detect co-localization.

• Analysis: Employ multichannel color profiling and quantitative co-localization analysis using software such as ImageJ with the JaCoP plugin.

This approach has successfully demonstrated SLC35C1 co-localization with specific subcellular compartments while showing its absence from lysosomes and mitochondria .

What methodologies are most effective for quantifying SLC35C1 expression changes in experimental settings?

For precise quantification of SLC35C1 expression changes, researchers should employ a multi-method approach:

• Real-time PCR (qPCR):

  • Extract total RNA using standard protocols

  • Synthesize cDNA using reverse transcriptase

  • Perform qPCR with SLC35C1-specific primers

  • Normalize to reference genes (e.g., GAPDH, β-actin)

  • Analyze using the 2^(-ΔΔCT) method

• Western blotting:

  • Extract proteins using appropriate lysis buffers

  • Separate proteins by SDS-PAGE

  • Transfer to membranes and probe with SLC35C1 antibody (#ab60336, Abcam)

  • Quantify band intensities using ImageJ software

  • Normalize to loading controls (e.g., β-actin)

• Immunohistochemistry quantification:

  • Perform IHC as described in question 2.1

  • Capture multiple representative images

  • Use digital image analysis software to quantify staining intensity

  • Apply H-score or other semi-quantitative scoring systems

• Bioinformatic analysis of public datasets:

  • Access TCGA data through tools like UALCAN or cBioPortal

  • Extract transcripts per million (TPM) values

  • Perform statistical analysis using appropriate tests (t-test, ANOVA)

  • Evaluate correlations between SLC35C1 and other genes of interest

This multi-method approach provides robust validation of expression changes across different experimental systems and has been successfully employed to document SLC35C1 downregulation in colon cancer .

How can genome editing techniques be optimized for studying SLC35C1 function in cellular models?

Researchers can optimize genome editing approaches to study SLC35C1 function by implementing these methodological strategies:

• CRISPR-Cas9 system:

  • Design multiple sgRNAs targeting exonic regions of SLC35C1

  • Clone into appropriate vectors (e.g., LentiCRISPR V2)

  • Validate editing efficiency using T7 endonuclease assay

  • Screen clones by sequencing and SLC35C1 antibody-based Western blotting

  • Confirm complete loss of function through fucosylation assays

• TALENs approach:

  • Design TALEN pairs targeting SLC35C1 coding regions

  • Transfect target cells and select clones

  • Validate knockout efficiency by sequencing and Western blotting

  • Assess functional consequences through phenotypic assays

• ZFNs method:

  • Design zinc-finger nucleases specific to SLC35C1

  • Deliver to target cells and isolate clones

  • Confirm gene disruption through molecular techniques

  • Evaluate SLC35C1 protein absence using specific antibodies

• Validation of knockout effects:

  • Perform rescue experiments by reintroducing wild-type SLC35C1

  • Analyze cellular phenotypes, including:

    • Cell proliferation assays

    • Colony formation in soft agar

    • Wnt signaling activity using TOPFLASH assay

    • Expression of Wnt target genes (C-myc, Axin2, Cyclin D1)

This comprehensive approach has been successfully applied to generate SLC35C1-deficient cells for studying its role in Wnt signaling and to create CHO cell lines capable of producing fucose-free antibodies .

What are the most sensitive methods for detecting alterations in SLC35C1-mediated fucosylation using specific antibodies?

To detect alterations in SLC35C1-mediated fucosylation with high sensitivity, researchers should consider these advanced methodological approaches:

• Lectin-based detection systems:

  • Use fucose-specific lectins (e.g., Aleuria aurantia lectin, AAL)

  • Combine with SLC35C1 antibody staining in dual-labeling experiments

  • Perform flow cytometry analysis to quantify fucosylation levels

  • Include positive controls (normal cells) and negative controls (SLC35C1-knockout cells)

• Mass spectrometry glycomics:

  • Isolate N-glycans from SLC35C1-normal and -deficient cells

  • Perform MALDI-TOF MS or LC-MS/MS analysis

  • Quantify fucosylated versus non-fucosylated glycan structures

  • Correlate findings with SLC35C1 expression levels determined by antibody-based methods

• Antibodies against fucosylated epitopes:

  • Use antibodies that specifically recognize fucosylated structures (e.g., Lewis X)

  • Perform comparative analysis between SLC35C1-normal and -silenced cells

  • Quantify by flow cytometry, ELISA, or immunoblotting

  • Validate specificity with fucosidase treatment controls

• Functional assays for fucosylation:

  • Assess incorporation of GDP-[³H]fucose in cell-free systems

  • Measure cellular uptake of fluorescent fucose analogs

  • Correlate with SLC35C1 protein levels detected by antibodies

  • Conduct immunoprecipitation of SLC35C1 followed by transporter activity assays

These methods provide complementary approaches to link SLC35C1 protein expression with its functional role in mediating fucosylation, which is essential for understanding both normal physiological processes and pathological conditions such as cancer development and progression .

How can SLC35C1 antibodies be utilized in protein interaction studies to elucidate Wnt signaling regulation?

SLC35C1 antibodies can be strategically employed in protein interaction studies to investigate its role in Wnt signaling regulation through the following methodological approaches:

• Co-immunoprecipitation (Co-IP):

  • Prepare cell lysates from normal and SLC35C1-manipulated cells

  • Immunoprecipitate using SLC35C1 antibodies

  • Analyze precipitated complexes for Wnt pathway components

  • Perform reverse Co-IP with antibodies against suspected interacting partners

  • Validate interactions using overexpressed tagged versions of SLC35C1

• Proximity ligation assay (PLA):

  • Co-label fixed cells with SLC35C1 antibody and antibodies against Wnt pathway components

  • Apply species-specific PLA probes

  • Visualize interaction signals as fluorescent spots

  • Quantify interactions under various experimental conditions

• Bimolecular fluorescence complementation (BiFC):

  • Generate fusion constructs of SLC35C1 and potential interactors with split fluorescent protein fragments

  • Transfect into appropriate cell lines

  • Analyze reconstituted fluorescence as evidence of protein interaction

  • Validate with antibody-based detection of expression levels

• Chromatin immunoprecipitation (ChIP) analysis:

  • Perform ChIP using antibodies against β-catenin and TCF/LEF transcription factors

  • Analyze occupancy at Wnt target gene promoters

  • Compare between SLC35C1-normal and -deficient cells

  • Correlate with expression changes in Wnt target genes (C-myc, Axin2, Cyclin D1)

• Secretome analysis:

  • Collect conditioned media from SLC35C1-normal and -silenced cells

  • Immunoprecipitate Wnt ligands using specific antibodies

  • Quantify secreted Wnt proteins (e.g., Wnt3a) by Western blotting

  • Correlate with functional Wnt activity using TOPFLASH reporter assays

This multi-faceted approach has revealed that SLC35C1 reduction increases Wnt3a secretion and elevates Wnt target gene expression, establishing SLC35C1 as a negative regulator of the canonical Wnt pathway .

What is the significance of SLC35C1 downregulation in colorectal cancer progression?

The downregulation of SLC35C1 in colorectal cancer has significant implications for disease progression and potential therapeutic interventions:

• Correlation with cancer stages:

  • SLC35C1 shows decreased expression across all stages of colon cancer as demonstrated by immunohistochemistry and TCGA database analysis

  • Real-time PCR confirms reduced SLC35C1 mRNA levels specifically in stage 3 and stage 4 colorectal cancer tissues

  • This progressive downregulation correlates with advancing disease stage, suggesting its involvement in cancer progression

• Relationship with Wnt pathway activation:

  • SLC35C1 functions as a negative regulator of the canonical Wnt signaling pathway

  • Its reduction leads to increased β-catenin activity, as evidenced by TOPFLASH reporter assays

  • Analysis of the TCGA database reveals a negative correlation between SLC35C1 mRNA levels and β-catenin expression (Pearson: -0.10, Spearman: -0.10, P = 0.0276)

  • This correlation supports the mechanistic link between SLC35C1 downregulation and Wnt pathway overactivation in colorectal carcinogenesis

• Cellular consequences:

  • Reduced SLC35C1 significantly promotes cell proliferation in HEK293 cells

  • SLC35C1 silencing enhances colony formation in soft agar assays, indicating increased tumorigenic potential

  • Mechanistically, SLC35C1 reduction elevates the mRNA levels of Wnt target genes (C-myc, Axin2, and Cyclin D1)

  • SLC35C1 knockdown increases secretion of Wnt3a ligand, providing a potential mechanism for Wnt pathway activation

• Potential as biomarker and therapeutic target:

  • The consistent downregulation of SLC35C1 across colorectal cancer stages suggests its potential utility as a diagnostic biomarker

  • Therapeutic strategies aimed at restoring SLC35C1 function might help normalize Wnt signaling and potentially inhibit cancer progression

  • This represents a novel approach to targeting the Wnt pathway, which is abnormally activated in approximately 90% of colorectal cancers

The significant negative correlation between SLC35C1 levels and β-catenin expression, combined with functional studies demonstrating its impact on cell proliferation and Wnt target gene expression, establish SLC35C1 downregulation as an important contributor to colorectal cancer development through Wnt pathway dysregulation .

How can researchers develop experimental models to study the therapeutic potential of restoring SLC35C1 function in cancer?

Researchers can develop comprehensive experimental models to investigate the therapeutic potential of restoring SLC35C1 function in cancer using these methodological approaches:

• In vitro overexpression systems:

  • Generate stable cell lines with inducible SLC35C1 expression in colorectal cancer cells

  • Utilize lentiviral vectors containing full-length SLC35C1 cDNA under doxycycline-inducible promoters

  • Confirm expression using SLC35C1-specific antibodies via Western blotting and immunofluorescence

  • Assess phenotypic changes including:

    • Cell proliferation rates

    • Colony formation ability

    • Migration and invasion capacity

    • Wnt pathway activity using TOPFLASH reporter assays

• In vivo xenograft models:

  • Implant SLC35C1-overexpressing cancer cells in immunocompromised mice

  • Compare with control cancer cells (expressing empty vector)

  • Monitor tumor growth, invasion, and metastasis

  • Analyze tumor tissues for Wnt target gene expression

  • Evaluate potential therapeutic efficacy through:

    • Tumor growth inhibition

    • Survival extension

    • Metastasis reduction

• Pharmacological approaches:

  • Screen compound libraries for molecules that enhance SLC35C1 expression or activity

  • Validate hits using reporter systems that monitor SLC35C1 promoter activity

  • Confirm increased SLC35C1 protein levels via antibody-based detection methods

  • Assess functional consequences on:

    • GDP-fucose transport

    • Protein fucosylation patterns

    • Wnt signaling activity

    • Cancer cell phenotypes

• Clinical correlation studies:

  • Analyze patient-derived tumor samples for SLC35C1 expression using validated antibodies

  • Correlate expression levels with:

    • Clinical outcomes

    • Treatment responses

    • Wnt pathway activation markers

    • Tumor recurrence and patient survival

  • Identify patient subgroups most likely to benefit from SLC35C1-targeting strategies

• Combination therapy models:

  • Test SLC35C1 restoration in combination with established anti-cancer therapies

  • Evaluate potential synergistic effects with:

    • Conventional chemotherapeutics

    • Targeted Wnt pathway inhibitors

    • Immunotherapy approaches

  • Determine optimal treatment regimens and sequences

These experimental models provide a comprehensive framework for evaluating the therapeutic potential of restoring SLC35C1 function as a novel approach to inhibit Wnt signaling in colorectal and potentially other cancers where this pathway is dysregulated .

What are the implications of SLC35C1 manipulation for producing fucose-free antibodies in biotechnology applications?

The manipulation of SLC35C1 presents significant implications for producing fucose-free antibodies in biotechnology applications, particularly for enhanced therapeutic efficacy:

• Enhanced antibody effector functions:

  • Removal of core fucose from N-glycans attached to human IgG1 significantly enhances its affinity for the FcγRIII receptor

  • This structural modification dramatically improves antibody-dependent cellular cytotoxicity (ADCC) activity

  • Fucose-free antibodies exhibit 50-100 fold increased ADCC compared to their fucosylated counterparts

• Genome editing approaches for SLC35C1 inactivation:

  • Multiple genome editing technologies have been successfully applied to inactivate SLC35C1 in Chinese hamster ovary (CHO) cells:

    • Zinc Finger Nucleases (ZFNs)

    • Transcription Activator-Like Effector Nucleases (TALENs)

    • CRISPR-Cas9 system

  • These approaches provide alternative strategies to the previously established method of inactivating fucosyltransferase 8 (FUT8)

  • The resulting SLC35C1-knockout CHO cell lines can be used as production platforms for fucose-free therapeutic antibodies

• Methodological advantages of targeting SLC35C1:

  • Targeting the GDP-fucose transporter (SLC35C1) affects all fucosylation processes by limiting substrate availability

  • This approach can potentially be more efficient than targeting individual fucosyltransferases

  • The strategy may result in more complete defucosylation of produced antibodies

  • Validation of fucose absence can be performed using:

    • Lectin blotting with fucose-specific lectins

    • Mass spectrometry glycan analysis

    • Functional assays measuring ADCC activity

• Production considerations:

  • SLC35C1-knockout cell lines must be thoroughly characterized for:

    • Growth characteristics and viability

    • Protein production capacity and stability

    • Product quality attributes beyond fucosylation

    • Long-term genetic stability

• Therapeutic applications:

  • Fucose-free antibodies produced in SLC35C1-deficient cells may offer advantages in:

    • Cancer immunotherapy (enhanced tumor cell killing)

    • Autoimmune disease treatment (improved clearance of pathogenic cells)

    • Infectious disease therapy (enhanced neutralization of pathogens)

The strategic inactivation of the SLC35C1 gene in CHO cells represents an alternative and potentially superior approach for generating production cell lines capable of producing therapeutic antibodies with enhanced effector functions, offering significant benefits for next-generation antibody therapeutics .

How might SLC35C1 antibodies be utilized in developing novel cancer diagnostic tools?

SLC35C1 antibodies show significant potential for developing innovative cancer diagnostic tools through several methodological approaches:

• Multiplex immunohistochemistry panels:

  • Combine SLC35C1 antibodies with markers for Wnt pathway activation (β-catenin, TCF/LEF)

  • Develop algorithmic scoring systems based on SLC35C1 downregulation patterns

  • Create tissue microarray-based screening platforms for early cancer detection

  • Correlate staining patterns with clinical outcomes to establish prognostic value

• Liquid biopsy applications:

  • Develop assays to detect SLC35C1 levels in circulating tumor cells (CTCs)

  • Create antibody-based capture systems for CTCs with altered SLC35C1 expression

  • Design immunoassays for detecting soluble SLC35C1 or associated biomarkers in patient serum

  • Monitor treatment response through longitudinal assessment of these markers

• Imaging diagnostics:

  • Generate radiolabeled or fluorescently tagged SLC35C1 antibodies for in vivo imaging

  • Develop contrast agents that target cells with altered SLC35C1/fucosylation patterns

  • Create dual-modality probes combining SLC35C1 targeting with functional Wnt activity sensors

  • Establish protocols for monitoring therapy response through longitudinal imaging

• Multi-parameter diagnostic algorithms:

  • Integrate SLC35C1 expression data with:

    • Genomic profiling (mutations in APC, KRAS, TP53)

    • Glycomics analysis of fucosylation patterns

    • Wnt pathway activation signatures

    • Clinical parameters

  • Develop machine learning models to enhance diagnostic accuracy and prognostic prediction

• Companion diagnostics for targeted therapies:

  • Create standardized SLC35C1 immunoassays to identify patients likely to respond to:

    • Wnt pathway inhibitors

    • Fucosylation-targeting therapies

    • Combined treatment approaches

  • Establish clinical cutoff values for treatment decision-making

The observed consistent downregulation of SLC35C1 across all stages of colorectal cancer, combined with its functional relationship to Wnt pathway dysregulation, positions it as a promising biomarker for incorporation into next-generation cancer diagnostic platforms .

What are the technical challenges in developing highly specific SLC35C1 antibodies for research and diagnostic applications?

Developing highly specific SLC35C1 antibodies presents several technical challenges that researchers must address through methodological refinements:

• Epitope selection challenges:

  • SLC35C1 is a multi-pass transmembrane protein with limited exposed extracellular domains

  • The protein shares structural similarities with other SLC35 family transporters

  • Critical functional domains may be conformationally sensitive or masked

  • Optimal strategy requires:

    • Careful bioinformatic analysis to identify unique, accessible epitopes

    • Design of peptide antigens from both hydrophilic and transmembrane regions

    • Generation of antibodies against multiple epitopes for comprehensive detection

• Antibody validation requirements:

  • Standard validation approaches may be insufficient due to SLC35C1's complex localization

  • Comprehensive validation protocol should include:

    • Testing in SLC35C1 knockout/knockdown models as negative controls

    • Demonstration of specific staining in tissues with known expression patterns

    • Confirmation of expected subcellular localization (Golgi, ER, endosomes)

    • Correlation of immunodetection with mRNA expression data

    • Evaluation across multiple experimental platforms (WB, IHC, IF, FACS)

• Cross-reactivity considerations:

  • Antibodies must distinguish SLC35C1 from other GDP-sugar transporters

  • Potential cross-reactivity with:

    • SLC35A1 (CMP-sialic acid transporter)

    • SLC35A2 (UDP-galactose transporter)

    • SLC35A3 (UDP-N-acetylglucosamine transporter)

    • Other fucose metabolism-related proteins

  • Requires extensive cross-reactivity testing against related proteins

• Detection sensitivity issues:

  • SLC35C1 may be expressed at low levels in certain tissues

  • Downregulation in cancer further reduces target abundance

  • Enhancement strategies include:

    • Signal amplification methods (tyramide signal amplification, polymer detection systems)

    • Optimization of antigen retrieval protocols for fixed tissues

    • Development of capture enhancement techniques for low-abundance samples

• Application-specific optimization:

  • Different applications require tailored antibody characteristics:

    • Western blotting: recognition of denatured epitopes

    • Immunohistochemistry: compatibility with fixation methods

    • Immunoprecipitation: affinity for native protein

    • Flow cytometry: recognition of extracellular epitopes (if any)

  • Each application requires specific validation and optimization protocols

Addressing these technical challenges through systematic development and rigorous validation is essential for creating SLC35C1 antibodies with the specificity and sensitivity required for reliable research and diagnostic applications across diverse experimental platforms .

How can integrative multi-omics approaches enhance our understanding of SLC35C1 function in health and disease?

Integrative multi-omics approaches offer powerful strategies to comprehensively elucidate SLC35C1 function in health and disease contexts through these methodological frameworks:

• Integrated genomics-transcriptomics analysis:

  • Correlate SLC35C1 genetic variations with expression patterns across:

    • Cancer vs. normal tissues

    • Different cancer stages and subtypes

    • Various tissue and cell types

  • Analyze TCGA and other large-scale datasets to identify:

    • Expression quantitative trait loci (eQTLs) affecting SLC35C1

    • Co-expression networks linking SLC35C1 to functional pathways

    • Potential transcriptional regulators of SLC35C1

  • Implement machine learning algorithms to predict functional consequences of SLC35C1 variants

• Proteomics-glycomics integration:

  • Combine SLC35C1 protein expression data with comprehensive glycomic profiling

  • Correlate SLC35C1 levels with:

    • Global fucosylation patterns

    • Site-specific glycan alterations on individual proteins

    • Changes in glycoprotein function and stability

  • Employ advanced mass spectrometry methods to link SLC35C1 activity with:

    • Protein-specific fucosylation changes

    • Altered glycoprotein interactions and signaling

    • Modified cellular glycosylation pathways

• Functional multi-omics:

  • Implement CRISPR-based SLC35C1 perturbation combined with:

    • RNA-seq to identify transcriptional consequences

    • Proteomics to detect protein expression changes

    • Glycomics to map altered fucosylation patterns

    • Metabolomics to assess impact on cellular metabolism

  • Analyze data using systems biology approaches to construct comprehensive regulatory networks

• Spatial multi-omics integration:

  • Apply multiplexed immunofluorescence with SLC35C1 antibodies alongside:

    • Cell type-specific markers

    • Wnt pathway components

    • Fucosylated protein detection

  • Implement spatial transcriptomics to map SLC35C1 expression in tissue context

  • Correlate with glycan imaging techniques to visualize fucosylation patterns in situ

• Clinical multi-omics:

  • Integrate SLC35C1 expression data with:

    • Patient genomic profiles

    • Tumor glycomic signatures

    • Treatment responses

    • Clinical outcomes

  • Develop predictive models for:

    • Cancer progression risk based on SLC35C1 status

    • Therapeutic response prediction

    • Patient stratification for personalized treatment approaches

This integrative multi-omics framework enables a comprehensive understanding of SLC35C1's complex roles in fucosylation, Wnt signaling regulation, and cancer development, potentially revealing novel diagnostic and therapeutic opportunities that would be missed by single-omic approaches .

What are the optimal antibody concentrations and experimental conditions for different SLC35C1 detection methods?

What is the expression profile of SLC35C1 across different cancer types and stages?

What are the quantitative effects of SLC35C1 manipulation on Wnt pathway components and cell phenotypes?

What are the common technical issues encountered when working with SLC35C1 antibodies and how can they be addressed?

How can researchers optimize co-expression analysis of SLC35C1 with Wnt pathway components?

What quality control measures should be implemented when evaluating SLC35C1 antibodies for research applications?