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Introduction
Protein glycosylation is an enzymatically regulated process in which glycans are attached to specific amino acid residues of proteins, predominantly occurring in the endoplasmic reticulum (ER) and Golgi apparatus. Major forms of protein glycosylation include N‑linked glycosylation and O‑linked glycosylation, which differ in their attachment sites and biological functions. Glycosylation plays essential roles in regulating protein folding, stability, trafficking, and function, as well as diverse biological processes such as cell adhesion, cell communication, and immune response. Aberrant glycosylation patterns are closely associated with various pathological conditions, including cancer, inflammation, and autoimmune disorders.
Products Solutions
Our glycosylation solutions integrate targeted O‑GlcNAc detection and enrichment with high‑throughput glycoprotein and glycan profiling, providing flexible tools for glycosylation analysis across different research stages.
- Specific O‑GlcNAc detection
- Efficient modification enrichment
- High‑throughput glycoprotein profiling
- Broad glycan pattern analysis
| Product Type | Product Name | Catalog No. |
|---|---|---|
| Rabbit pAb | Pan‑O‑GlcNAc Rabbit pAb | WT9013 |
| Rabbit mAb | Pan‑O‑GlcNAc Rabbit mAb | WT9014 |
| Rabbit mAb | Pan‑O‑GlcNAc Rabbit mAb | WT9145R |
| Rabbit mAb | Pan‑O‑GlcNAc Rabbit mAb‑BSA and Azide free | WT9123 |
| Rabbit mAb | O‑Linked N‑Acetylglucosamine MultiPTM Rabbit Monoclonal Antibody mix | WT9014M |
| Agarose Conjugated | O‑GlcNAc Specific Antibody Conjugated Agarose Beads | WT9156B |
| Motif Kit | O‑GlcNAc (GlcNAc‑S/T) Motif Kit | WT911K |
| Array | Human Glycosylation Array 1000 | WT9609A‑1000‑4 |
| Array | Human Glycosylation Array 1000 | WT9609A‑1000‑8 |
| Array | Human Glycosylation Array 1000B | WT9609A‑1000B‑4 |
| Array | Human Glycosylation Array 1000B | WT9609A‑1000B‑8 |
| Array | Human Glycosylation Array 493 | WT9609A‑493‑4 |
| Array | Human Glycosylation Array 493 | WT9609A‑493‑8 |
| Array | Human Glycosylation Array 507 | WT9609A‑507‑4 |
| Array | Human Glycosylation Array 507 | WT9609A‑507‑8 |
| Array | Human Glycosylation Array 8000 | WT9609A‑8000‑4 |
| Array | Human Glycosylation Array 8000 | WT9609A‑8000‑8 |
| Array | Human Glycosylation Array L3 | WT9609A‑L3‑4 |
| Array | Human Glycosylation Array L3 | WT9609A‑L3‑8 |
| Array | Human Glycosylation Array L4 | WT9609A‑L4‑4 |
| Array | Human Glycosylation Array L4 | WT9609A‑L4‑8 |
Research Areas
- Protein activity and stability
- Cell signaling and communication
- Cellular stress response
- Immune response
References
- He M, Zhou X, Wang X. Glycosylation: mechanisms, biological functions and clinical implications. Signal Transduct Target Ther. 2024;9(1):194. Published 2024 Aug 5.
- Chen L, Zhou Q, Zhang P, et al. Direct stimulation of de novo nucleotide synthesis by O‑GlcNAcylation. Nat Chem Biol. 2024;20(1):19‑29.
- Fu L, Yin K, Xu X, Wu R. Systematic Quantification of Protein O‑GlcNAcylation Reveals Common and Cell‑Type‑Specific Responses to N‑Glycosylation Inhibition in Human Cells. Anal Chem. 2026;98(21):15689‑15699.