On the other hand, O-mannosyl glycans of α-Dg have been analyzed in a number of studies ( Chiba et al., 1997 Harrison et al., 2012 Inamori et al., 2012a Nakamura et al., 2010b Stalnaker et al., 2010 Yoshida-Moriguchi et al., 2010), and these glycans have been demonstrated to play crucial roles in the development and physiology of the nervous system and muscles (reviewed in ( Muntoni et al., 2011 Nakamura et al., 2010a Stalnaker et al., 2011b)). However, the structure-function relationship of O-mannosylation of proteins other than α-Dg remains unknown. This conclusion is consistent with recent glycomic analyses that indicated that α-Dg represents just a minor component of the O-mannosylated glycoproteome of mouse brain ( Stalnaker et al., 2011a). Previous studies suggested that other O-mannosylated glycoproteins likely exist ( Finne et al., 1979 Krusius et al., 1986 Wing et al., 1992 Yuen et al., 1997). Other confirmed targets of this modification include CD24, a mouse GPI-linked cell adhesion molecule that functions in the nervous and immune systems ( Bleckmann et al., 2009), neurofascin, a neuronal cell adhesion molecule involved in the nervous system development and neural transmission ( Pacharra et al., 2012), and IgG2 light chain antibody recombinantly expressed in Chinese hamster ovary cell culture ( Martinez et al., 2007). O-mannose-linked structures have been reported on receptor tyrosine phosphatase β (RPTPβ) that mediates cell signaling and regulates neural cell adhesion and migration ( Abbott et al., 2008). The presence of O-mannosylation has been demonstrated for Drosophila Dystroglycan and its glycosylation has been analyzed by in vitro and in vivo approaches ( Nakamura et al., 2010b). More recent research in vertebrate and invertebrate species has significantly expanded our knowledge of O-mannosyl glycan structures and glycoproteins bearing this unique type of glycosylation ( Fig. Despite the fact that O-mannosyl glycans appear to be present on a number of glycoproteins, until now α-Dystroglycan (α-Dg) represents the only well-studied functional target of this modification ( Chiba et al., 1997 Stalnaker et al., 2011b). Protein O-mannosylation is an evolutionarily conserved type of glycosylation found in a wide range of metazoans, from insects to humans. This review will describe recent methodological strategies for studying protein O-mannosylation using in vitro and in vivo approaches. Protein O-mannosylation is evolutionarily conserved in metazoans, yet this pathway is simplified and more amenable to genetic analyses in invertebrate organisms, indicating that genetically tractable in vivo models could facilitate research in this area. However, this mechanism is underlain by complex genetic and molecular regulation that remain poorly understood. Recent progress in mass spectrometry and in vitro analyses has shed new light the mechanism of α-Dystroglycan glycosylation. Genetic defects of O-mannosylation result in the loss of ligand binding activity of α-Dystroglycan and causes congenital muscular dystrophies termed dystroglycanopathies. A major biological effect of O-mannosylation concentrates on the regulation of α-Dystroglycan, a membrane glycoprotein mediating cell – extracellular matrix interactions. Includes base, 2 cassettes to hold 1-2 lunches or up to 4 mini blotter sandwiches, blotter roll.Protein O-mannosylation is a special type of glycosylation that plays prominent roles in metazoans, affecting development and physiology of the nervous system and muscles. Environmentally friendly - environmentally friendly consumables eliminate disposal costs. Flexible design - allows user to customize transfer conditions and is compatible with traditional semi-dry consumables. Superior transfer efficiency - higher transfer efficiency than other protein transfer methods. ![]() Features and Benefits of the Trans-Blot Turbo Transfer System: - Fast blot transfer - 3 minute transfers of mini or midi gels - High throughput - can transfer 1-4 mini gels or 1-2 midi gels in one operation. ![]() ![]() Consumables for protein blotting are available in ready-to-use, pre-packaged stacks or in bulk quantities requiring assembly. Trans-Blot Turbo Transfer Packs include an optimized combination of buffer, membrane, and filter paper that provides superior transfers when paired with the Trans-Blot Turbo blotting device. The system enables protein transfer in just 3 minutes without sacrificing performance compared to traditional in-tank protein transfer. ![]() The Trans-Blot Turbo Transfer System is a high performance western blotting transfer system designed to provide rapid transfers with high efficiency.
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