Sialyl-Tn Antigen Inhibitor Development Service
Sialyl-Tn Antigen Inhibitor Development Service at CD BioGlyco
The biosynthetic pathway of sialyl-Tn antigen involves the interaction of multiple enzymes and substrates. UDP-N-Acetylglucosamine (UDP-GlcNAc) is catalyzed by β-1,3-N-acetylglucosaminyltransferase and combines with N-acetylgalactosamine (GalNAc) residues in O-glycoprotein to form Tn antigen. The Tn antigen will be further catalyzed by core 1 synthase to transfer the galactose (Gal) residue to the Tn antigen to form an O-sugar chain of the core 1 structure (Galβ1-3GalNAcα-Ser/Thr). Finally, members of the sialyltransferase enzyme family catalyze the transfer of sialic acid (Neu5Ac) to the O-glycan chain of the core 1 structure, thereby forming the sialyl-Tn antigen. Sialyl-Tn is a pan-cancer antigen expressed early in tumorigenesis. The development of sialyl-Tn antigen inhibitors interferes with the biosynthesis process of sialyl-Tn antigen, which is of great significance to cancer research and other fields.
CD BioGlyco has diverse Glycosylation Inhibitor Development Solutions, and we provide multiple modes of sialyl-Tn antigen inhibitor development services.
- Antibody development service
CD BioGlyco uses immunological technology to develop sialyl-Tn antibodies with high affinity and specificity, which selectively bind and clear sialyl-Tn antigens, such as two anti-STn mAbs (TKH2 and HB-STn1), new anti-STn antibodies (LLU9B4 and 3P9). At the same time, we also provide production for the developed antibodies using different technologies.
- Mouse hybridoma technology
CD BioGlyco fuses B cells stimulated by sialyl-Tn antigen with cancer cells (such as malignant myeloma cells) to form hybridoma cells, which produce monoclonal antibodies (mAb) against sialyl-Tn antigen.
- Recombinant antibody technology
CD BioGlyco clones and expresses sialyl-Tn antibody gene fragments, and then produces large quantities of recombinant antibodies in bacterial, yeast, or mammalian expression systems. This method produces antibodies on a large scale with high consistency and repeatability.
- mAb technology
CD BioGlyco uses the RNA or DNA of a single cell to extract the sialyl-Tn antibody gene sequence from immune cells and performs gene cloning, expression, and purification.
- Phage display technology
CD BioGlyco inserts the sialyl-Tn antibody gene library into the phage surface display to identify and select specific antibodies by screening phage particles that bind the sialyl-Tn antigen.
- Small molecule inhibitor development service
CD BioGlyco also conducts screening on enzymes involved in the synthesis of sialyl-Tn antigen through high-throughput screening or computer-assisted methods. We design and optimize the small molecule compounds obtained from the screening to interfere with the synthesis or recognition of sialyl-Tn antigen.
In addition, CD BioGlyco uses cell or animal models to evaluate the inhibitory effect and safety of the developed antibodies and candidate molecules using techniques such as ELISA, western blot, and flow cytometry to determine their mechanism of action against the sialyl-Tn antigen. We provide high-quality sialyl-Tn antigen inhibitor assessment services.
Fig.1 Sialyl-Tn antigen inhibitor development service. (CD BioGlyco)
Publication
Technology: mAb technology
Journal: Journal of Immunotherapy
IF: 4.912
Published: 2013
Results: The authors developed 3P9, a tumor suppressor monoclonal antibody against colorectal cancer that targeted the cancer-associated antigen sialyl-Tn. The authors used mAb3P9 to treat mice with tumors and calculated the tumor volume (A) and weight (B), the results showed that mAb3P9 inhibited tumor growth in vivo and induced apoptosis of tumor cells.
Fig.2 Tumor cell volume and weight results. (An, et al., 2013)
Applications
- Cancer research: The expression of sialyl-Tn antigen is increased in various cancers and is related to tumor invasion, metastasis, and prognosis. The development of sialyl-Tn antigen inhibitors interferes with the expression or binding of this antigen, thereby blocking the growth, metastasis, and drug resistance of tumor cells.
- Immunotherapy research: Sialyl-Tn antigen is used as a tumor-specific antigen to induce the body's immune response. By developing sialyl-Tn antigen inhibitors, the antigenicity of sialyl-Tn antigen may be reduced, and the immune attack on normal cells may be reduced.
- Vaccine design: Sialyl-Tn antigen plays an important role in viral and bacterial infections, affecting the recognition and clearance of pathogens by the host immune system. By developing sialyl-Tn antigen inhibitors, it is possible to interfere with the binding or interaction of the antigen with pathogens, provide new strategies for vaccine design, and enhance immune response and protective effects.
Advantages
- Mature technology means: CD BioGlyco has mature technology means that support key steps such as research on antigen-inhibitor interactions, high-throughput screening, and optimization of candidate compounds.
- Drug design and synthesis capabilities: Our expert team has professional knowledge and experience in drug design and organic synthesis, and carries out inhibitor design, synthesis, and structural optimization of sialyl-Tn antigens.
- Efficient activity assessment: We perform an efficient assessment of the activity of candidate inhibitors to ensure the efficacy and safety of candidate compounds.
CD BioGlyco has a strong scientific research team who are familiar with the latest research progress and technology in inhibitor development fields. We have rich experience in the development of sialyl-Tn antigen inhibitors and provide clients with high-quality sialyl-Tn antigen inhibitor development services. Please feel free to contact us for specific details if you require quality inhibitor development service.
References
- Loureiro, L.R.; et al. Challenges in antibody development against Tn and sialyl-Tn antigens. Biomolecules. 2015, 5(3): 1783-1809.
- An, Y.; et al. A novel anti-sTn monoclonal antibody 3P9 inhibits human xenografted colorectal carcinomas. Journal of Immunotherapy. 2013, 36(1): 20-28.
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