Abstract: The present invention refers to the use of antibodies against the Thomsen-Friedenreich (TF) as reagents for in vitro diagnostics of Microsatellite Instability (MSI). Another aspect of this invention refers to a method for the in vitro diagnostics of MSI comprising the said composition employing the anti-TF antigen antibodies and measuring the expression of the TF antigen in a tissue sample. The present invention further refers to a kit comprising the above mentioned compositions for detecting MSI by conducting the present invention's method. The use, composition, methods and kit may be advantageously applied to significantly facilitate the identification of MSI in the clinical setting through a single marker-based sensitive and specific detection of MSI in patients with cancers of gastric, colorectal and other tissues for diagnostics, prognostics or prediction of response to treatment.

Abstract: The invention provides several molybdenum (II) complexes (see classes I and II, FIG. 1) as well as pharmaceutical compositions comprising these compounds, that are useful for treating cancer and describes synthetic methods and intermediates useful for preparing the compounds.

Abstract: Attachment of O-glycans to proteins is controlled by a large family of homologous polypeptide GalNAc-transferases. Polypeptide GalNAc-transferases contain a C-terminal sequence with similarity to lectins. This invention discloses that the putative lectin domains of GalNAc-transferase isoforms, GalNAc-T4, -T7, -T2, and -T3, are functional and recognize carbohydrates, glycopeptides, and peptides and discloses the lectin domains of GalNAc-T1-T16. These lectin domains have different binding specificities and modulate the functions of GalNAc-transferase isoforms differently. Novel methods for identification of inhibitors or modulators of binding activities mediated by lectin domains of polypeptide GalNAc-transferases are disclosed. Direct binding activity of GalNAc-transferase lectins has been demonstrated for the first time and methods to measure lectin mediated binding of isolated lectins or enzymes with lectin domains are disclosed.

Abstract: Attachment of O-glycans to proteins is controlled by a large family of homologous polypeptide GalNAc-transferases. Polypeptide GalNAc-transferases contain a C-terminal sequence with similarity to lectins. This invention discloses that the putative lectin domains of GalNAc-transferase isoforms, GalNAc-T4, -T7, -T2, and -T3, are functional and recognize carbohydrates, glycopeptides, and peptides and discloses the lectin domains of GalNAc-T1-T16. These lectin domains have different binding specificities and modulate the functions of GalNAc-transferase isoforms differently. Novel methods for identification of inhibitors or modulators of binding activities mediated by lectin domains of polypeptide GalNAc-transferases are disclosed. Direct binding activity of GalNAc-transferase lectins has been demonstrated for the first time and methods to measure lectin mediated binding of isolated lectins or enzymes with lectin domains are disclosed.