Anti-GALNTL2 antibody [EPR11580]

Supplementary info

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

Activity summary

GALNTL2 also known as Polypeptide N-Acetylgalactosaminyltransferase-like 2 is an enzyme that belongs to the polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family. This enzyme has a molecular mass of approximately 63 kDa. It plays an important mechanical role in the initiation of mucin-type O-glycosylation by transferring N-acetylgalactosamine to the hydroxyl group of serine or threonine residues on target proteins. These modifications are essential for protein function. GALNTL2 is widely expressed in different human tissues including the liver brain and heart indicating its involvement in various physiological processes.

Biological function summary

The enzyme acts by modifying proteins to mediate their stability signaling and interaction with other molecules. GALNTL2 functions within a complex network of enzymes that manage glycosylation processes contributing to the modification of a variety of substrates. By altering protein structures through glycosylation it affects cell signaling pathways and immune responses. The enzyme's ability to modulate proteins influences processes like cellular adhesion and communication which are essential for maintaining tissue integrity and function.

Pathways

GALNTL2 plays a role in the O-glycosylation pathway which is important for proper protein folding and function. This pathway intersects with the protein processing pathway in the endoplasmic reticulum. GALNTL2 acts in conjunction with other members of the GalNAc-T family including GALNT1 and GALNT2 to fine-tune the glycosylation of proteins that pass through the secretory pathway. These processes are important for orchestrating responses to cellular stress and maintaining cellular homeostasis.

Associated diseases and disorders

GALNTL2's dysfunction can relate to certain cancers and metabolic disorders. Abnormal glycosylation patterns due to mutations or misregulations in GALNTL2 have associations with cancer progression particularly in pathways involving cell-cell communication and adhesion influencing tumor growth and metastasis. Additionally metabolic disorders such as diabetes might also involve GALNTL2 through its interactions with signaling molecules like insulin. These associations highlight the importance of studying GALNTL2 for therapeutic targets in disease treatment.