Anti-ALG2 antibody [EPR12006(2)(B)]

Supplementary info

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

Activity summary

The ALG2 protein also known as asparagine-linked glycosylation 2 plays a role in the early steps of N-glycan precursor biosynthesis. ALG2 has a molecular mass of approximately 51 kDa and shows expression in multiple tissues including the liver and brain. The protein acts mechanically to facilitate the addition of the first mannose residue to the lipid-linked oligosaccharide (LLO) precursor in the endoplasmic reticulum a fundamental step in protein glycosylation processes.

Biological function summary

Certain processes depend on the actions of ALG2. This protein becomes part of the larger oligosaccharyltransferase complex where it ensures proper glycosylation of nascent proteins—a modification important for protein folding and stability. ALG2 modulates the efficiency of protein maturation by its role in glycan formation affecting how proteins interact within cellular processes. Defects in ALG2 lead to improper protein folding and cellular distribution.

Pathways

ALG2 functions as an important component in the protein glycosylation pathway and more specifically in the N-glycan assembly pathway. This protein interacts closely with other glycosylation enzymes like ALG12 which further add branches to the glycans once ALG2 completes its function. The interactions within this pathway ensure proper biological functionalization of glycoproteins facilitating diverse roles from cell signaling to immune recognition.

Associated diseases and disorders

ALG2 mutations have known associations with congenital disorders of glycosylation (CDG) a group of diseases caused by defects in glycosylation. Such mutations can cause a spectrum of developmental and metabolic issues. ALG2 dysfunction linked to proteins like ALG9 in co-regulatory roles reveals the impact of glycosylation on cellular homeostasis. These insights into ALG2 give promise for potential therapeutic targets in managing CDG symptoms and advancing understanding of glycosylation-related pathology.