alpha 1 Mannosidase 1A: Lysates
a1,2-Mannosidase IA is a Type II transmembrane Golgi-resident enzyme that belongs to class I a1,2-Mannosidases (glycosylhydrolase family 47). a1,2-Mannosidases plays an essential role in the maturation of N-glycans to hybrid and complex oligosaccharides in mammalian cells. Class I a1,2- Mannosidases are conserved through evolution. They can be classified into three subgroups according to their enzymatic activities. The first subgroup includes yeast and human endoplasmic reticulum (ER) a1,2-Mannosidases that primarily trim Man9GlcNAc2 to Man8GlcNAc2 isomer B. The second subgroup includes mammalian Golgi a1,2-Mannosidases IA, IB, and IC that trim Man9GlcNAc2 to Man5GlcNAc2 through Man8GlcNAc2 isomer A and C. These Golgi mannosidases display different tissue- and cell-specific expression, subcellular localization, and substrate specificity. The third subgroup includes yeast and mammalian proteins that do not hydrolyze Man9GlcNAc2. Proteins from subgroup 1 and 3 have been implicated in ER quality control and in proteasomal degradation of misfolded glycoproteins. It was also suggested that Golgi mannosidases from the second subgroup may play a role in the ERAD (endoplasmic reticulum-associated degradation) of defective glycoproteins 1-5. Although a1,2-Mannosidase IA is predominantly detected in the juxtanuclear Golgi region by indirect immunofluorescence, significant cell type and speciesdependent variation in localization was reported. The pig liver enzyme has been localized to the ER and transitional vesicles between ER and Golgi, but is not found within the Golgi stacks of porcine hepatocytes.
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alpha 1 Mannosidase 1A: Lysates
a1,2-Mannosidase IA is a Type II transmembrane Golgi-resident enzyme that belongs to class I a1,2-Mannosidases (glycosylhydrolase family 47). a1,2-Mannosidases plays an essential role in the maturation of N-glycans to hybrid and complex oligosaccharides in mammalian cells. Class I a1,2- Mannosidases are conserved through evolution. They can be classified into three subgroups according to their enzymatic activities. The first subgroup includes yeast and human endoplasmic reticulum (ER) a1,2-Mannosidases that primarily trim Man9GlcNAc2 to Man8GlcNAc2 isomer B. The second subgroup includes mammalian Golgi a1,2-Mannosidases IA, IB, and IC that trim Man9GlcNAc2 to Man5GlcNAc2 through Man8GlcNAc2 isomer A and C. These Golgi mannosidases display different tissue- and cell-specific expression, subcellular localization, and substrate specificity. The third subgroup includes yeast and mammalian proteins that do not hydrolyze Man9GlcNAc2. Proteins from subgroup 1 and 3 have been implicated in ER quality control and in proteasomal degradation of misfolded glycoproteins. It was also suggested that Golgi mannosidases from the second subgroup may play a role in the ERAD (endoplasmic reticulum-associated degradation) of defective glycoproteins 1-5. Although a1,2-Mannosidase IA is predominantly detected in the juxtanuclear Golgi region by indirect immunofluorescence, significant cell type and speciesdependent variation in localization was reported. The pig liver enzyme has been localized to the ER and transitional vesicles between ER and Golgi, but is not found within the Golgi stacks of porcine hepatocytes.
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| Applications: | WB |