MCC Antibody, Biotin conjugated

What is MCC protein and what are its biological functions?

MCC (Colorectal mutant cancer protein) functions primarily as a tumor suppressor that inhibits cell proliferation in colorectal cancer. Specifically, it suppresses the Wnt/β-catenin pathway by inhibiting DNA binding of β-catenin/TCF/LEF transcription factors. MCC is also involved in cell migration independently of RAC1, CDC42, and p21-activated kinase (PAK) activation .

Recent research has revealed that MCC represses the canonical Wnt signaling pathway in a CCAR2-dependent manner. It accomplishes this by sequestering CCAR2 to the cytoplasm, which impairs CCAR2's ability to inhibit SIRT1. This is significant because SIRT1 plays a role in deacetylating β-catenin, thereby negatively regulating its transcriptional activity . These multiple functions make MCC antibodies valuable tools for studying colorectal cancer mechanisms and Wnt signaling regulation.

Why use biotin-conjugated antibodies for MCC detection?

Biotin conjugation offers several methodological advantages for MCC detection. The biotin-streptavidin interaction features an extremely low dissociation constant (kd) of 4 × 10^-14 M, making it one of the strongest non-covalent interactions in nature . This high affinity ensures stable and reliable detection systems.

The advantages of biotin conjugation for MCC antibodies include:

• Signal amplification: A single biotinylated antibody can bind multiple streptavidin molecules, each carrying reporter molecules, enhancing detection sensitivity.

• Flexibility: Biotin-conjugated MCC antibodies can be paired with various streptavidin-conjugated reporter molecules (fluorophores, enzymes, etc.) without requiring multiple antibody conjugates.

• Preservation of functionality: When conjugation is specifically targeted to the Fc region of the antibody (as with ZBPA methods), the binding capacity of the antibody remains largely unaffected .

• Multiplexing capability: Biotin-conjugated MCC antibodies can be combined with other detection systems for simultaneous analysis of multiple targets.

Which detection methods work best with biotin-conjugated MCC antibodies?

Based on the available research, biotin-conjugated MCC antibodies have demonstrated effectiveness in several detection methods:

• Enzyme-Linked Immunosorbent Assay (ELISA): The primary validated application, with both research sources confirming compatibility . ELISA provides quantitative data on MCC expression levels with high sensitivity.

• Immunohistochemistry (IHC): When properly conjugated using methods like ZBPA, biotin-conjugated antibodies show excellent performance in tissue detection, enabling precise localization of MCC protein . The method provides distinct immunoreactivity without off-target staining, making it ideal for studying MCC expression patterns in cancer tissues.

• Enzyme Immunoassay (EIA): Confirmed as a viable application for biotin-conjugated MCC antibodies .

For optimal results in IHC applications, researchers should consider using detection systems that mitigate potential endogenous biotin interference, particularly when examining tissues known to have high endogenous biotin levels (like liver, kidney, and brain).

How does biotinylation affect MCC antibody performance?

The impact of biotinylation on MCC antibody performance depends significantly on the conjugation method employed. Research comparing different biotinylation techniques has revealed important differences:

• Site-specific conjugation (like ZBPA methods): When biotin is specifically attached to the Fc portion of the antibody, the variable regions that determine antigen binding remain unmodified. This preserves the antibody's binding characteristics and specificity . Studies have shown that ZBPA-biotinylated antibodies maintained expected staining patterns without introducing background staining.

• Non-specific conjugation (like Lightning-Link): When biotinylation occurs at random sites throughout the antibody, including potentially in the antigen-binding regions, binding affinity and specificity may be compromised. Research has shown that non-specifically biotinylated antibodies often produce additional background staining patterns that do not correspond to the expected protein localization .

What are the main biotinylation techniques for MCC antibodies?

Several biotinylation methods are applicable to MCC antibodies, each with distinct characteristics:

• Z-domain of Protein A (ZBPA) conjugation: This method utilizes a modified Z-domain from staphylococcal protein A that specifically targets the Fc region of antibodies. The Z-domain contains benzoylphenylalanine (BPA), which forms covalent bonds with amino acids upon UV exposure. Biotin is incorporated into the protein domain during solid-phase peptide synthesis, ensuring precise positioning . This method provides highly specific conjugation without affecting the antibody's binding regions.

• Lightning-Link conjugation: A commercial kit that targets amine or carboxyl groups on proteins. While quick and convenient, this method is non-specific, potentially labeling both the variable and constant regions of antibodies as well as any stabilizing proteins present in the solution .

• Glyco-conjugation: This method targets carbohydrate moieties on antibodies, typically through oxidation of terminal sugar residues to create aldehyde functionalities for biotin attachment. This approach provides site-specific conjugation without significantly altering the antibody's binding properties .

• Site-specific cysteine incorporation: This involves introducing a solvent-accessible cysteine into the antibody scaffold, providing a specific handle for conjugation. After expression and reduction to remove existing adducts, the mutant antibodies can be functionalized with biotin using thiol-reactive chemistry .

For MCC antibodies specifically, comparative studies suggest ZBPA conjugation provides superior results for applications requiring high specificity and low background.

How does ZBPA biotinylation compare to standard amine-coupling methods?

Research directly comparing ZBPA biotinylation with standard amine-coupling methods (such as Lightning-Link) for antibody preparation shows significant differences in performance:

In a direct comparison study with 14 different antibodies, all ZBPA-biotinylated antibodies showed distinct immunoreactivity without off-target staining, regardless of the presence of stabilizing proteins in the buffer. In contrast, the majority of Lightning-Link biotinylated antibodies displayed characteristic patterns of non-specific staining .

For MCC antibody research, especially in complex tissues where background interference could complicate interpretation, the ZBPA method offers superior specificity despite requiring more specialized reagents.

What is the optimal antibody concentration for successful biotinylation?

The optimal antibody concentration varies by conjugation method:

When working with precious or low-concentration MCC antibodies, the ZBPA method offers advantages, though researchers should anticipate some loss of material during the conjugation and purification process.

How can I verify successful biotinylation of my MCC antibody?

Verification of successful biotinylation is crucial before employing MCC antibodies in experimental procedures. Several methods can be used:

• Streptavidin shift assay: Mix a small amount of biotinylated antibody with streptavidin and run on non-reducing SDS-PAGE. Successfully biotinylated antibodies will form higher molecular weight complexes with streptavidin, causing a visible shift in the gel.

• HABA assay (4'-hydroxyazobenzene-2-carboxylic acid): This colorimetric assay measures biotin concentration based on the displacement of HABA from avidin by biotin, resulting in a measurable absorbance change. This method allows quantification of the average number of biotin molecules per antibody.

• Mass spectrometry: For precise determination of biotinylation sites and efficiency, mass spectrometry analysis can identify modified peptides after protease digestion.

• Functional verification: Perform a small-scale pilot experiment comparing the biotinylated MCC antibody with the unconjugated version using identical samples. For IHC applications, this should reveal whether the staining pattern remains consistent with expected MCC localization patterns. Research has shown that properly biotinylated antibodies should maintain the same tissue and cellular specificity as their unconjugated counterparts .

For MCC antibodies specifically, comparison with established staining patterns in positive control tissues (such as colorectal tissues) can provide confidence in successful and functional biotinylation.

How do I optimize signal-to-noise ratio when using biotin-conjugated MCC antibodies?

Optimizing signal-to-noise ratio is crucial for obtaining reliable results with biotin-conjugated MCC antibodies. Several strategies can be employed based on research findings:

• Conjugation method selection: Research demonstrates that ZBPA-biotinylated antibodies consistently produce lower background staining compared to non-specifically biotinylated antibodies . For MCC detection in tissues with high endogenous biotin or complex protein environments, selecting a site-specific conjugation method is crucial.

• Blocking endogenous biotin: Use avidin/biotin blocking kits before applying biotinylated antibodies, particularly when working with tissues known to have high endogenous biotin (liver, kidney, brain). Sequential application of avidin followed by biotin effectively blocks endogenous biotin and any remaining biotin-binding sites.

• Optimization of antibody concentration: Titrate the biotinylated MCC antibody to determine the optimal concentration that maximizes specific signal while minimizing background. Studies have shown that post-conjugation filtration to remove free biotin may not significantly impact background if the background is caused by non-specifically labeled proteins rather than excess free biotin .

• Use of appropriate controls: Include biotinylated isotype controls and secondary-only controls to distinguish between specific binding and background signal. For MCC specifically, comparing staining patterns with unconjugated antibodies using indirect detection can help validate the specificity of the biotinylated version.

• Detection system optimization: When using streptavidin-based detection systems, titrate the streptavidin conjugate to avoid signal oversaturation or excessive background due to non-specific binding.

What controls should be included in experiments using biotin-conjugated MCC antibodies?

Comprehensive control strategies are essential for validating results with biotin-conjugated MCC antibodies:

• Unconjugated antibody control: Include the same MCC antibody clone in its unconjugated form using standard indirect detection methods. This establishes the baseline staining pattern for comparison. Research has shown that properly biotinylated antibodies should maintain the same localization patterns as their unconjugated counterparts .

• Isotype control: Use a biotinylated isotype-matched control antibody that has undergone the same conjugation procedure to identify any background resulting from non-specific binding of the antibody class rather than antigen specificity.

• Negative controls:

  • Secondary reagent only: Apply only the streptavidin detection reagent without primary antibody to identify background from the detection system.

  • Known negative tissue: Include tissues known not to express MCC (based on established literature) to confirm specificity.

• Positive controls: Include tissues with established MCC expression patterns. For MCC, appropriate positive controls would include specific regions of colorectal tissues where MCC expression has been well-documented.

• Blocking controls: For biotin conjugates specifically, include controls where endogenous biotin is blocked versus unblocked to assess the contribution of endogenous biotin to observed signals.

• Buffer protein controls: If suspecting non-specific biotinylation of buffer proteins, run parallel experiments with biotinylated buffer components (e.g., albumin, gelatin) without antibody to identify potential background patterns. Research has shown that non-specifically biotinylated albumin and gelatin can produce characteristic background staining patterns in certain tissues .

How can I perform multiplexed detection involving MCC and other Wnt pathway components?

Multiplexed detection of MCC alongside other Wnt pathway components can provide valuable insights into pathway regulation. Several methodological approaches are available:

• Sequential multiplexing using biotin-based detection:

  • Apply the first antibody (biotinylated) and detect with a colored chromogen

  • Perform heat-based or chemical elution to remove the first set of reagents

  • Apply the second antibody (also biotinylated) and detect with a different colored chromogen

  • This approach works best with careful optimization of elution conditions to ensure complete removal of previous antibodies

• Parallel multiplexing using distinct detection systems:

  • Apply biotinylated MCC antibody detected with streptavidin-enzyme conjugate

  • Simultaneously or sequentially apply another antibody detected with a different system (e.g., alkaline phosphatase polymer)

  • This approach avoids cross-reactivity between detection systems

• Fluorescence multiplexing:

  • Apply biotinylated MCC antibody detected with fluorophore-conjugated streptavidin

  • Apply additional antibodies directly conjugated to other fluorophores or detected with species-specific secondary antibodies

  • This approach allows visualization of multiple targets in the same section with distinct fluorescence channels

• Z-domain conjugation with different reporter molecules:

  • Research indicates that the Z-domain conjugation method can be adapted to incorporate molecules other than biotin

  • By conjugating different antibodies with distinct reporter molecules, dual IHC can be performed even with antibodies from the same species

For studying MCC's interaction with other Wnt pathway components like β-catenin, careful selection of compatible detection systems is essential to avoid false colocalization signals.

What are the best approaches for quantitative analysis using biotin-conjugated MCC antibodies?

Quantitative analysis using biotin-conjugated MCC antibodies requires rigorous methodological considerations:

• For ELISA/EIA quantification:

  • Establish standard curves using recombinant MCC protein at known concentrations

  • Ensure consistent biotinylation levels between antibody batches by using the same conjugation protocol

  • Include replicate measurements and determine the coefficient of variation

  • Calculate the limit of detection and limit of quantification for the specific assay setup

• For immunohistochemistry quantification:

  • Use digital image analysis with standardized acquisition settings

  • Employ commercial or open-source software for consistent analysis

  • Consider using H-score method (intensity × percentage of positive cells) for semi-quantitative assessment

  • Include reference standards on each slide for normalization between experiments

• For flow cytometry:

  • Use antibody titration to determine optimal signal-to-noise ratio

  • Include quantitative beads with known binding capacity to convert fluorescence intensity to molecules of equivalent soluble fluorochrome (MESF)

  • Prepare consistent controls to establish positive and negative gates

• For all quantitative applications:

  • Verify the linear range of detection for your specific experimental setup

  • Include standard/reference samples across all experimental batches for normalization

  • Calculate and report coefficient of variation for technical and biological replicates

When quantifying MCC in relation to Wnt pathway activity, consider using parallel measurements of established Wnt target genes to correlate MCC levels with pathway activity metrics.

How can I reduce background staining when using biotin-conjugated MCC antibodies?

Background staining is a common challenge when using biotin-conjugated antibodies. Research findings provide several effective strategies:

• Conjugation method optimization: Studies comparing biotinylation methods found that ZBPA conjugation resulted in significantly less background staining compared to non-specific conjugation methods. For all 14 antibodies tested in one study, ZBPA biotinylation produced distinct immunoreactivity without off-target staining, while most Lightning-Link biotinylated antibodies showed characteristic non-specific staining patterns .

• Blocking protocols:

  • Apply avidin-biotin blocking steps prior to incubation with biotinylated antibodies

  • Use protein-based blockers (like 5% BSA, casein, or commercial protein blocks) to reduce non-specific binding

  • Include detergents (0.1-0.3% Triton X-100 or Tween-20) in washing buffers to reduce hydrophobic interactions

• Sample preparation:

  • Ensure complete antigen retrieval optimization for your specific tissue type

  • Block endogenous peroxidase activity before applying detection reagents

  • Use freshly prepared or properly stored tissues to minimize autofluorescence and non-specific binding

• Antibody dilution optimization:

  • Perform systematic titration of the biotinylated MCC antibody

  • Research indicates that higher antibody concentrations may increase background, especially with non-specific conjugation methods

• Filtration after conjugation:

  • Although removing free biotin through filtration may not always eliminate background (as shown in one study ), it remains a good practice to remove unconjugated components

For MCC antibodies specifically, attention to these details is particularly important when examining tissues with complex structures or high endogenous biotin content.

What should I do if my biotin-conjugated MCC antibody shows reduced binding capacity?

Reduced binding capacity after biotinylation is a common issue that can be addressed through several methodological approaches:

• Assess conjugation efficiency: Over-biotinylation can interfere with antigen binding, especially if biotin molecules are attached to or near the antigen-binding regions. Consider using methods that quantify the biotin:antibody ratio (like HABA assay) to ensure optimal conjugation.

• Investigate alternative conjugation methods: Research has shown that site-specific conjugation methods like ZBPA preserve binding capacity better than random amine-coupling methods . If using a commercial kit with reduced results, consider switching to a more site-directed approach.

• Adjust antibody concentration: Studies have noted that loss of antibody during filtration steps following conjugation can lead to apparently reduced staining intensity . Compensate by using a higher concentration of the biotinylated antibody compared to the unconjugated version.

• Optimize antigen retrieval: Different biotinylation methods may subtly affect antibody binding kinetics, requiring adjustment of antigen retrieval conditions. Systematically test different antigen retrieval methods (heat-induced vs. enzymatic) and conditions (pH, duration).

• Consider dual biotin incorporation: Research suggests that incorporating two biotin molecules in the Z-domain could potentially double detection efficiency, enabling successful staining with lower antibody concentrations .

• Verify antibody stability: Some biotinylation procedures may impact antibody stability. Ensure proper storage conditions and consider adding stabilizing proteins (if compatible with your conjugation method) to maintain functionality over time.

How can I address potential interference from endogenous biotin?

Endogenous biotin can significantly interfere with detection systems using biotin-conjugated antibodies. Several methodological approaches can minimize this interference:

• Avidin-biotin blocking: Apply unconjugated avidin to bind endogenous biotin, followed by excess biotin to saturate remaining avidin binding sites before applying biotinylated antibodies. Commercial kits are available specifically for this purpose.

• Tissue-specific considerations: Tissues vary significantly in endogenous biotin content. Liver, kidney, brain, and adipose tissue typically contain high levels of endogenous biotin and may require more rigorous blocking protocols. For MCC studies focused on colorectal tissues, standard blocking may be sufficient, but studies involving multiple tissue types should account for this variation.

• Alternative detection systems: For tissues with particularly high endogenous biotin, consider alternative detection methods:

  • Direct fluorophore conjugation of primary antibodies

  • Polymer-based detection systems that don't rely on biotin-streptavidin interaction

  • Alternative tagging systems like DNP (dinitrophenyl) or digoxigenin

• Streptavidin vs. avidin: Streptavidin typically shows less non-specific binding compared to avidin due to its neutral isoelectric point and lack of carbohydrate modifications. Preferentially use streptavidin-based detection systems when working with tissues known to have high endogenous biotin.

• Control experiments: Include control sections processed with streptavidin detection reagents only (no biotinylated antibody) to visualize and quantify endogenous biotin signal. This allows for accurate differentiation between specific and non-specific signals.

What are common pitfalls when using biotin-conjugated MCC antibodies in cancer tissue samples?

Cancer tissue analysis using biotin-conjugated MCC antibodies presents several methodological challenges:

• Heterogeneous expression: MCC functions as a tumor suppressor, and its expression may vary significantly within and between tumor samples. This heterogeneity requires careful interpretation of negative staining, which could represent either true absence of expression or technical limitations.

• Non-specific binding in necrotic regions: Necrotic areas in tumor samples often exhibit increased non-specific binding. Research has shown that non-specifically biotinylated proteins can produce characteristic background staining patterns . Carefully exclude these regions from analysis or use dual staining approaches to confirm specificity.

• Reduced antigenicity in fixed tissues: Formalin fixation can mask MCC epitopes, particularly affecting antibodies targeting conformational epitopes. Optimize antigen retrieval methods specifically for MCC detection in your tissue type and fixation protocol.

• Altered expression in cancer contexts: MCC regulates the Wnt/β-catenin pathway, which is frequently dysregulated in colorectal cancers. Consider the biological implications when interpreting MCC expression patterns in tumor versus normal tissue.

• Cross-reactivity with other proteins: In cancer tissues with altered protein expression profiles, potential cross-reactivity may occur. Always validate findings using alternative detection methods or antibodies targeting different epitopes of MCC.

• Endogenous biotin variation: Cancer cells often exhibit altered metabolism, potentially affecting endogenous biotin levels. Include appropriate controls to account for this variation when comparing normal versus malignant tissues.

• Interpretation challenges: As MCC is a putative tumor suppressor, interpreting its expression requires correlation with other markers of the Wnt pathway. Consider multiplexed approaches to simultaneously visualize MCC alongside β-catenin or other pathway components for comprehensive analysis.

How can biotin-conjugated MCC antibodies be used to study Wnt/β-catenin pathway inhibition?

Biotin-conjugated MCC antibodies offer powerful tools for investigating MCC's role in Wnt/β-catenin pathway inhibition through several methodological approaches:

• Co-immunoprecipitation studies: Biotinylated MCC antibodies can be used to pull down MCC protein complexes using streptavidin beads, followed by analysis of interacting partners including β-catenin, CCAR2, and SIRT1. This approach helps elucidate the molecular mechanisms by which MCC represses the Wnt pathway in a CCAR2-dependent manner .

• Chromatin immunoprecipitation (ChIP): Biotinylated MCC antibodies can be employed to investigate MCC's presence at β-catenin/TCF/LEF target gene promoters, helping to understand how MCC inhibits DNA binding of these transcription factors .

• Proximity ligation assays: Using biotinylated MCC antibodies alongside antibodies against other pathway components enables visualization of protein-protein interactions in situ through rolling circle amplification, providing spatial information about where in the cell these interactions occur.

• Sequential IHC analysis: Biotin-conjugated MCC antibodies can be used in sequential staining protocols to visualize MCC alongside β-catenin localization in the same tissue section. This approach helps correlate MCC expression with β-catenin nuclear localization (an indicator of active Wnt signaling).

• Quantitative pathway activity assessment: By combining MCC staining with quantitative analysis of Wnt target gene expression (through RNA in situ hybridization or multiplexed immunofluorescence), researchers can correlate MCC levels with pathway activity in clinical samples.

These approaches provide mechanistic insights into how MCC fulfills its tumor suppressor function through Wnt pathway inhibition, potentially revealing therapeutic vulnerabilities in colorectal cancers with altered MCC expression.

What are the latest approaches for studying MCC's role in cell migration using biotin-conjugated antibodies?

Advanced methodologies for investigating MCC's role in cell migration using biotin-conjugated antibodies include:

• Live-cell imaging: Biotinylated MCC antibodies can be used with cell-permeable streptavidin-fluorophore conjugates to visualize MCC localization during migration in real-time, helping elucidate its role independent of RAC1, CDC42, and PAK activation .

• Proximity biotinylation: Techniques like BioID or APEX2 can be combined with MCC-specific antibodies to identify proteins in close proximity to MCC during migration, revealing context-specific interaction networks.

• Super-resolution microscopy: Biotin-conjugated MCC antibodies paired with streptavidin-fluorophore probes enable super-resolution techniques like STORM or PALM to visualize MCC's subcellular localization at nanometer resolution during migration processes.

• Ratiometric imaging: By combining biotinylated MCC antibodies with antibodies against migration markers, researchers can create ratiometric maps showing the relationship between MCC expression and migratory behavior in complex tissues.

• Microfluidic migration assays: Biotinylated MCC antibodies can be incorporated into microfluidic systems to perform immunostaining on migrating cells subjected to defined chemical gradients, correlating MCC expression with directional migration properties.

These approaches help understand MCC's non-canonical functions beyond Wnt pathway regulation, potentially revealing new therapeutic strategies targeting migration-dependent processes in cancer progression.

How can biotin-conjugated MCC antibodies be integrated into single-cell analysis workflows?

Integration of biotin-conjugated MCC antibodies into single-cell analysis provides powerful insights into heterogeneous expression patterns:

• Single-cell proteomics:

  • Mass cytometry (CyTOF): Biotinylated MCC antibodies can be detected with streptavidin conjugated to rare earth metals for high-dimensional protein profiling at single-cell resolution

  • CODEX multiplexed imaging: Using DNA-barcoded streptavidin to detect biotinylated MCC antibodies allows integration into highly multiplexed imaging panels

• Spatial transcriptomics integration:

  • Sequential immunofluorescence and in situ sequencing: Biotin-conjugated MCC antibodies can be used in initial protein staining, followed by in situ RNA analysis

  • Spatial proteogenomics: Combining biotinylated MCC antibody staining with spatial transcriptomics methods like Visium or Slide-seq correlates protein expression with transcriptional profiles

• Single-cell pathway analysis:

  • Phospho-flow cytometry: Biotinylated MCC antibodies can be incorporated into phospho-flow panels to correlate MCC expression with activation states of Wnt and migration-related signaling pathways

  • Single-cell western blot: Biotin-conjugated antibodies can be integrated into microfluidic single-cell western blot workflows to analyze MCC alongside other pathway components

• Live-cell applications:

  • Cell sorting based on MCC expression: Biotinylated antibodies with cell-permeable fluorescent streptavidin conjugates can enable isolation of cells based on intracellular MCC expression

  • Single-cell secretion analysis: For secreted variants, biotinylated antibodies can be incorporated into single-cell secretion assays to correlate MCC secretion with cellular phenotypes

These approaches help resolve heterogeneous expression patterns of MCC in complex tissues and cell populations, particularly relevant for understanding tumor heterogeneity in colorectal cancers.

What are emerging applications for biotin-conjugated MCC antibodies in cancer biomarker research?

Biotin-conjugated MCC antibodies are finding novel applications in cancer biomarker research through several innovative methodological approaches:

• Liquid biopsy development:

  • Biotinylated MCC antibodies can be immobilized on magnetic beads for capture and enrichment of circulating tumor cells expressing MCC

  • Integration into multiplexed detection systems for simultaneous analysis of MCC alongside other Wnt pathway components in plasma or serum samples

• Extracellular vesicle (EV) analysis:

  • Biotin-conjugated MCC antibodies can be used to capture and characterize tumor-derived EVs containing MCC protein

  • Multiplexed EV profiling combining MCC with other markers to develop signatures predictive of colorectal cancer progression

• High-throughput screening applications:

  • Development of MCC-based functional assays using biotinylated antibodies for screening compounds that modulate MCC's tumor suppressor function

  • Integration into drug discovery workflows targeting the Wnt pathway in colorectal cancer

• Diagnostic assay development:

  • Creation of multiplexed diagnostic panels combining MCC with other colorectal cancer markers using biotin-streptavidin chemistry for signal amplification

  • Development of rapid point-of-care tests utilizing the high sensitivity of biotin-streptavidin detection systems

• Theranostic applications:

  • Using biotin-conjugated MCC antibodies for both diagnostic imaging and therapeutic delivery

  • Development of streptavidin-based nanocarriers loaded with therapeutic agents that can be targeted to MCC-expressing cells

These emerging applications leverage the specificity of MCC antibodies and the versatility of biotin-streptavidin chemistry to develop new approaches for colorectal cancer detection, monitoring, and treatment.