Abnormal glycosylation is a hallmark of cancer. Several carbohydrate structures are highly expressed in cancerous cells compared to normal tissue, including the Tn (GalNAcα1-O-Ser/Thr), STn (Neu5Acα2-6GalNAcα1-O-Ser/Thr) and T (Galβ1,3-GalNAcα1-O-Ser/Thr antigens (1,2). Antibodies to these can act as markers for cancerous cells (3) and have been used as the platform for diagnostics, therapeutics, and anti-cancer vaccines (4-6).
The Tn, STn and T antigen are often components of mucin protein, which are upregulated in cancerous cells (7). Mucins are large glycoproteins, either secreted from or membrane-bound in epithelial cells, in which O-linked oligosaccharides comprise more than 50% of the molecule by weight (8). They are up-regulated in cancerous cells and their localization changes from being on the apical side of normal epithelium to symmetrically distributed in malignantly transformed epithelium (Bos). Mucins are often abnormally glycosylated in cancerous cells and tissues (3, 7-9).
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SBH Sciences is looking for partners to investigate our glycosyltransferase enzymes and carbohydrate antibodies as diagnostic tools, therapeutics or for production of glycol-peptide/glycol-protein products. Moreover, our extensive bioassay and in vitro biomarker analysis capabilities are available to support development of your product.
We are open for suggestions and would be pleased to hear from you.