638207-70-2

Upstream product

• 1125-88-8 benzaldehyde dimethyl acetal 
• 189561-75-9 N-Fmoc-(O-N-acetylgalactosaminyl)threonine tert-butyl ester 
• 4098-06-0 triacetyl-D-galactal 
• 196398-25-1 3,4,6-tri-O-acetyl-2-azido-2-deoxy-α/β-D-galactopyranosyl nitrate 
• 120791-77-7 N-(9H-fluoren-9-yl)-methoxycarbonyl-O-(3,4,6-tri-O-acetyl-2-azido-2-desoxy-α-D-galactopyranosyl)-1-threonine tert-butyl ester 
• 120791-76-6 N-fluorenylmethoxycarbonyl-threonine-tert-butyl ester 
• 73731-37-0 Fmoc-Thr-OH 
• 25878-60-8 D-galactose pentaacetate 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 67673-39-6 3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl bromide 
• 120173-56-0 N^α-(9-fluorenylmethoxycarbony)-O-(2-acetamido-2-deoxy-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-L-threonine tert-butyl ester 

Downstream Products

• 638207-71-3 N-fluorenylmethoxycarbonyl-O-(2-acetamido-4,6-O-benzylidene-2-desoxy-3-O-[2,3,4-tri-O-acetyl-6-O-benzyl-β-D-galactopyranosyl]-α-D-galactopyranosyl)-L-threonine tert-butyl ester 
• 1240035-76-0 Fmoc-Thr(β-2F-Ac3Gal-(1->3)-α-4,6-O-Bzn-GalNAc)-OtBu 
• 1191118-17-8 Fmoc-Thr(α-2F-Ac3Gal-(1->3)-α-4,6-O-Bzn-GalNAc)-OtBu 
• 1191118-29-2 N-(9H-fluoren-9-yl)-methoxycarbonyl-O-(2-acetamido-2-deoxy-4,6-O-benzylidene-3-O-[2,3,4-tri-O-acetyl-6-deoxy-6-fluoro-β-D-galactopyranosyl])-α-D-galactopyranosyl-L-threonine-tert-butyl ester 
• 1326307-07-6 C₅₂H₆₂N₂O₁₉ 
• 1240035-68-0 Fmoc-Thr(β-2F-Bn3Gal-(1->3)-α-4,6-O-Bzn-GalNAc)-OtBu 
• 638207-72-4 N-fluorenylmethoxycarbonyl-O-(2-acetamido-2-deoxy-4,6-O-benzylidene-3-O-[6-O-benzyl-β-D-galactopyranosyl]-α-D-galactopyranosyl)-L-threonine tert-butyl ester 
• 908349-09-7 N-(9H-fluoren-9-yl)methoxycarbonyl-O-(2-acetamido-2-deoxy-3-O-[2,3,4-tri-O-acetyl-6-O-benzyl-β-D-galactopyranosyl]-α-D-galactopyranosyl)-L-threonine-tert-butylester 

Relevant academic research and scientific papers

Synthetic vaccines consisting of tumor-associated MUC1 glycopeptide antigens and bovine serum albumin

(Chemical Equation Presented) Sweet medicine: The mucin MUC1 is highly overexpressed on epithelial tumor cells. Glycopeptides 1 (from the repeating unit of MUC1) carrying various important sialylated tumor-associated carbohydrate antigens R were synthesiz

Synthesis of Tn/T antigen MUC1 glycopeptide BSA conjugates and their evaluation as vaccines

The tumor-associated mucin MUC1 over-expressed in most epithelial tumor tissues is considered a promising target for immunotherapy. The extracellular part of MUC1 contains a domain of numerous tandem repeats of the amino acid sequence HGVTSAPDTRPAPGSTAPPA, including five potential O-glycosylation sites. In this study, T9 and S15 have been chosen as the positions of glycosylation. The glycopeptides N-terminally equipped with a triethylene glycol spacer were synthesized by microwave-assisted Fmoc solid-phase peptide synthesis. After detachment from the resin and deprotection, the MUC1 glycopeptides were conjugated to bovine serum albumin (BSA). To evaluate the immunological properties, balb/c mice were immunized with these BSA vaccines. Copyright

Synthesis and structural model of an α(2,6)-sialyl-T glycosylated MUC1 eicosapeptide under physiological conditions

To study the effect of O-glycosylation on the conformational propensities of a peptide backbone, a 20residue peptide (GSTAPPAHGVT-SAPDTRPAP) representing the full length tandem repeat sequence of the human mucin MUC1 and its analogue glycosylated with the

Biomimetic synthesis of the tumor-associated (2,3)-sialyl-T antigen and its incorporation into glycopeptide antigens from the mucins MUC1 and MUC4

Glycoproteins on epithelial tumor cells often exhibit aberrant glycosylation profiles. The incomplete formation of the glycan side chains resulting from a down-regulated glucosamine transfer and a premature sialylation results in additional peptide epitop

Synthetic Glycopeptides of the Tandem Repeat Sequence of the Epithelial Mucin MUC4 with Tumour-associated Carbohydrate Antigens

Glycohexadecapeptides representing the tandem repeat sequence of the epithelial mucin MUC4 were prepared by applying a solid-phase methodology. The required glycosyl amino acid building blocks containing the tumour-associated saccharide antigens TN/