ImmunoArrayᵀᴹ MUC1 Glycopeptide Microarray (CAT#: NA-0726-FY38)

The MUC1 Glycopeptide Microarray is a high-sensitivity, low-background profiling matrix engineered to decode antibody and protein interactions with the heavily modified tandem repeats of Mucin 1. Displaying 62 synthetic 23-mer glycopeptides structurally modified with truncated Tn and STn cancer-specific glycans-alongside an unglycosylated peptide reference-this high-throughput tool isolates precise epitopic binding preferences from minimal sample volumes. Operating as an essential platform for onco-glycomics and immunotherapy discovery, it enables translational medicine researchers to systematically screen serological autoantibodies, evaluate therapeutic antibody cross-reactivity, and dissect how structural alterations in the mucosal sugar coat dictate tumor immune tolerance and cancer progression.

Specifications
SizeMulti-array slide format featuring multiple identical sub-arrays per chip, enabling parallel multi-sample profiling. It accommodates a total of 63 target spots (62 glycopeptides + 1 unglycosylated peptide) plus controls.
Throughput LevelHigh-throughput (enables the parallel analysis of multiple samples on a single chip, facilitating rapid profiling of antibody or protein binding relationships in a single assay).
Arraying TechnologyMultiplex glycopeptide microarray technology where 63 specific MUC1 targets are orderly printed onto the sub-arrays of a solid slide surface; molecular binding events (such as the Bauhinia purpurea lectin [BPL] model resolved via biotin-streptavidin-Cy3 chemistry) are captured and measured using a microarray slide scanner at a 532 nm wavelength.
Quality ControlIntegrated positive controls are embedded within each sub-array layout to demonstrate expected target-ligand binding signals (such as verifying signature BPL lectin interaction with Tn-glycosylated sites), ensuring correct grid alignment and assay validity.
FeaturesTumor-Specific Epitope Focus: Specifically populated with Tn and STn short-chain modifications to represent the hypoglycosylated states typical of cancer-associated MUC1. High Sensitivity & Low Background: Highly optimized surface chemistry to isolate weak antibody-carbohydrate or protein-peptide affinities without non-specific noise. Built-in Structural Contrast: Includes an unglycosylated 23-mer peptide control to easily differentiate baseline peptide binding from true glycan-dependent interactions. Ultra-low Sample Volume: Employs a highly efficient micro-assay format requiring only minimal biological sample sizes. Customization & Service Support: Fully customizable to meet individual research goals, with professional companion assay screening and detection services available upon request.
Application FieldsSerological Autoantibody Screening: Screening patient sera for disease-related autoantibodies that bind specific tumor-associated MUC1 glycoforms, serving as a tool for early cancer diagnostics. Antibody Specificity Mapping: Characterizing, identifying, and comparing the carbohydrate-binding preferences and fine structural epitopes of targeted anti-MUC1 therapeutic monoclonal antibodies. Interactome Profiling: Evaluating the precise binding actions of MUC1-interacting host proteins, circulating extracellular vesicles, immune cells, and viral particles. Oncological Antigen Discovery: Investigating the abnormal O-glycosylation pathways (such as the loss of core-2 structures) that shield tumor cells from host immune surveillance, to support targeted vaccine and cell therapy development.
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For Research Use Only | Not For Clinical Use

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