When a virus infects mammalian host cells, glycan epitopes on the cell surface are exploited as virus receptors The surface of a virus particle is frequently modified with glycosylation in order to escape from an immunological host defense. For the study of virus-glycan interactions and infectious inhibition, TCI displays a line-up of oligosaccharide products containing virus-related glycan epitope structures.
8-Oxoadenosine [O0401], oxidized at the 8-position of adenosine as in 8-oxoguanosine, is found in RNA as a result of the nucleobase damage caused by reactive oxygen species in vivo. It is thought that such nucleobase damage causes mismatches during DNA replication and inhibition of RNA translation, leading to carcinogenesis, neurodegenerative diseases, and aging. These 8-oxo nucleosides have been considered to be generated in RNA more than in DNA, since DNA is protected by chromatin. In the study of the effects of rRNA oxidation on protein synthesis and structural stabilization of RNA, the site-specific introduction of oxidized nucleosides including 8-oxoadenosine into RNA has been reported.
Biotinylated Inhibitor for the Detection of Protein Activity by Stripping
Most peptide-type protease inhibitors interact with the active site of the protease. Once these inhibitors are bound to the protease, they must be removed from the protease by macro-dilution or protein denaturation. However, KNI1293 biotin [K0064], a biotinylated HIV-1 (human immunodeficiency virus type 1) protease inhibitor, can be removed (stripped) by streptavidin after binding to the protease. The biotinylated protease inhibitor-streptavidin binding shift phenomenon is expected to be used to study the activity of protease-related diseases.