Anti-GALNTL6 antibody

Supplementary info

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

Activity summary

GALNTL6 also known as Polypeptide N-acetylgalactosaminyltransferase-like protein 6 is an enzyme responsible for catalyzing the initial step of O-linked glycosylation. It transfers N-acetylgalactosamine (GalNAc) to serine and threonine residues of proteins. The molecular mass of GALNTL6 is approximately 72 kDa. Its expression is observed in several tissues including the brain and reproductive organs suggesting tissue-specific roles.

Biological function summary

GALNTL6 contributes to the regulation of protein glycosylation which impacts protein folding stability and signaling functions. It does not appear to be a part of a larger protein complex but functions as an individual glycosyltransferase enzyme. Through its glycosylating activities GALNTL6 influences cell-cell communication and adhesion processes especially within the cellular matrix.

Pathways

GALNTL6 plays a role in the biosynthetic pathway of O-linked glycan synthesis significantly affecting mucin-type O-glycosylation pathways. It relates to proteins such as mucins a family of high molecular weight heavily glycosylated proteins that play pivotal roles in forming protective mucous barriers. These processes are important for maintaining healthy epithelial surfaces and modulating interactions between cells and their environment.

Associated diseases and disorders

Aberrant glycosylation involving GALNTL6 has been linked to several conditions. Changes in its function or expression may contribute to disorders such as colorectal cancer and polycystic ovary syndrome (PCOS). In these disorders GALNTL6 is connected to alterations in other glycosylation-related proteins including MUC1 which is known to have altered glycosylation patterns in tumour progression and cancer metastasis. Understanding GALNTL6's involvement in these diseases could inform potential therapeutic strategies.