Anti-Mannosidase II/MAN2A1 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Mannosidase II also known as MAN2A1 is an enzyme that plays a mechanical role in the processing of N-linked oligosaccharides. It performs this task by cleaving mannose residues from glycoproteins during the process of glycan maturation. MAN2A1 has a mass of about 133 kDa and is predominantly located in the Golgi apparatus an important cellular organelle involved in modifying sorting and packaging proteins. This enzyme shows expression in various types of tissues contributing to different levels of glycoprotein processing in the human body.

Biological function summary

Mannosidase II is involved in glycoprotein maturation and functions as an important component within the N-glycan biosynthesis pathway. It does not form a permanent complex with other enzymes but interacts with other glycosylation enzymes to ensure sequential processing. This enzyme helps in maintaining the consistency and specificity of glycoprotein folding and function impacting cellular communication and stability. Various cells across tissues utilize glycoproteins for different cellular processes illustrating MAN2A1's importance in molecular biology.

Pathways

MAN2A1 plays a significant role in the N-glycan biosynthesis and quality control pathway. This pathway involves a cascade of enzymatic actions facilitating proper protein folding and cellular signaling. Within these pathways other essential proteins such as alpha-mannosidase I and N-acetylglucosaminyltransferase I work in tandem with mannosidase II. MAN2A1 contributes to the precision of glycosylation alterations affecting signal transductions and cell-cell interactions important in various physiological processes.

Associated diseases and disorders

MAN2A1 associates with congenital disorders of glycosylation and certain types of cancer including hepatocellular carcinoma. Improper function or expression of this enzyme can lead to aberrant glycosylation patterns contributing to these diseases. In cancer progression glycosylation changes influence cell adhesion and immune surveillance affecting tumor behavior and metastasis. MAN2A1 can indirectly interact with proteins like E-cadherin through altered glycosylation influencing cell-cell adhesion and cancer development.