MANEA
MANEA (mannosidase endo-alpha), also known as glycoprotein endo-alpha-1,2-mannosidase, FLJ12838 or mandaselin, is a Golgi-resident endomannosidase. It helps process N-linked glycans by cleaving alpha-1,2-mannosidic bonds that link glucosylated mannose oligosaccharides to high-mannose glycans. Browse Assay Genie's current range of MANEA research reagents below, or read on for the biology behind the target.
MANEA is an endomannosidase that acts in the Golgi during N-glycan maturation. N-glycosylation begins in the endoplasmic reticulum (ER), where an oligosaccharyltransferase complex transfers the preassembled oligosaccharide glucose-3-mannose-9-N-acetylglucosamine-2 from dolichyl pyrophosphate to acceptor sites on the target protein. This core oligosaccharide is then trimmed in sequence by several ER glycosidases and by an endomannosidase such as MANEA in the Golgi.
MANEA catalyses the release of mono-, di- and triglucosylmannose oligosaccharides by cleaving the alpha-1,2-mannosidic bond that links them to high-mannose glycans. This activity is classed as EC 3.2.1.130. The enzyme is a Golgi apparatus membrane protein and belongs to the glycosyl hydrolase 99 family. Studies of the MANEA gene and MANEA protein therefore bear on how glycoproteins are processed as they move through the secretory pathway.
The HGNC places the gene in the mannosidases endo-alpha group, and its previous name was mannosidase, endo-alpha. Other names in the literature include FLJ12838 and mandaselin. Mouse and rat both carry a Manea ortholog, which allows comparative work on glycan processing in common model organisms.
MANEA is an endomannosidase that trims the core oligosaccharide in the Golgi after ER glycosidases have acted, making it relevant to studies of glycoprotein maturation.
As a glycosyl hydrolase 99 family member that cleaves alpha-1,2-mannosidic bonds, MANEA is a subject for work on endomannosidase specificity and mechanism.
MANEA is a Golgi membrane enzyme, so it is useful for examining how glycan-processing steps are organised within the secretory pathway.
MANEA releases mono-, di- and triglucosylmannose oligosaccharides from high-mannose glycans, supporting investigation of glucosylated glycan turnover.
MANEA is a Golgi endomannosidase. It cleaves the alpha-1,2-mannosidic bond that links mono-, di- and triglucosylmannose oligosaccharides to high-mannose glycans, releasing them during N-glycan processing, after ER glycosidases have trimmed the core oligosaccharide.
MANEA stands for mannosidase endo-alpha. UniProt calls the protein glycoprotein endo-alpha-1,2-mannosidase. Aliases include FLJ12838 and mandaselin, and the previous HGNC name was mannosidase, endo-alpha. The enzyme is classified as EC 3.2.1.130.
Yes. Mouse and rat each have an ortholog named Manea, so the enzyme can be studied in rodent models. Check the datasheet of any product for its validated reactivity before choosing a reagent for a given species.
Other mannosidases, glucosidases and glycan-processing enzymes involved in N-glycosylation with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q5SRI9; product specifications from Assay Genie datasheets.