Available Sequences

Example 1 shows the binding interactions  on our MUC1 Glycopeptide Array slide that was assayed with a glycan-binding protein - biotinylated Bauhinia purpurea agglutinin (BPL) lectin.






Example 2 shows the binding interactions  on our MUC1 Glycopeptide Array slide that was assayed with a STn antibody. 

Typical Binding Events

Benefits:
Low background
High sensitivity
Small sample volume
Simple assay format
Affordable
Assay service available
Customizable

Applications:

  • Serological screening of disease-associated autoantibodies binding to MUC1 glycopeptides
  • Map unique MUC1 glycopeptide epitopes to determine carbohydrate specificities of antibodies
  • Evaluate binding specificities of MUC1-interacting proteins

For the MUC1 Glycopeptide Array user manual, click here.
To place an order, contact us at info@zbiotech.com or visit our online store.

Mucin 1 (MUC1) is a transmembrane glycoprotein, and it is one of several mucin proteins that make up mucus. The extracellular domain of MUC1 consists of a variable number of 20-amino-acid tandem repeats, and these repeats are highly O-glycosylated. α-N-acetylgalactosamine (GalNAc, Tn) is attached to the hydroxyl group of threonine (Thr) and serine (Ser) of the tandem repeats and further extended with galactose (Gal), N-acetylglucosamine (GlcNAc), or GalNAc to form eight different core structures. These structures can be further modified by sialylation, sulfation, acetylation, fucosylation, and polylactosamine extension.

MUC1 is expressed on the surface of normal epithelial cells. However, changes in glycosylation patterns occur in various pathological conditions. For example, aberrant glycosylation of MUC1 has prevented cancer cells from forming core-2-based glycans. Therefore, cancer-associated MUC1 is hypoglycosylated with short carbohydrate structures such as Tn (GalNAc-Ser or -Thr) and STn (Neu5Ac-6-GalNAc-Thr). This unique feature makes MUC1 an ideal cancer-specific antigen for therapeutics development.

Z Biotech has developed a robust chemoenzymatic synthesis and microarray platform that enables the production and screening of a large MUC1 glycopeptide library. The first version of our MUC1 glycopeptide array includes 62 MUC1 glycopeptides and 1 unglycosylated peptide. Each glycopeptide is 23-mer in length and modified with carbohydrate structures such as Tn (GalNAc-Ser or -Thr) or STn (Neu5Ac-6-GalNAc-Ser or -Thr). This array platform allows researchers to identify, profile and compare specific antibody responses; as well as detect and validate protein interactions with various glycoforms of MUC1 peptides. This microarray platform is highly sensitive and has low background by using our proprietary surface coating and glycan immobilization technology.

MUC1 Glycopeptide Array