CHST10 Human

CHST10 specifically catalyzes the transfer of sulfate to the 3-position of terminal glucuronic acid residues in both protein- and lipid-linked oligosaccharides . This sulfation process is essential for the proper functioning of various biological molecules and pathways. The enzyme uses 3’-phosphoadenosine-5’-phosphosulfate (PAPS) as the sulfate donor in this reaction .

The sulfation of carbohydrates by CHST10 is critical for several physiological processes, including cell signaling, molecular recognition, and the stabilization of extracellular matrices. Sulfated carbohydrates are involved in interactions with proteins such as growth factors, cytokines, and adhesion molecules, which are vital for cellular communication and immune responses .

Recombinant human CHST10 is produced using Chinese Hamster Ovary (CHO) cells, which are commonly used in biotechnology for the production of therapeutic proteins. The recombinant enzyme is typically expressed with a C-terminal 6-His tag to facilitate purification . The purified enzyme is then characterized for its activity, purity, and stability.

Recombinant CHST10 is used in various research applications to study the role of carbohydrate sulfation in biological processes. It is also utilized in the development of therapeutic agents targeting sulfation pathways. The enzyme’s activity can be measured by its ability to transfer sulfate from PAPS to phenolphthalein glucuronic acid, with specific activity values exceeding 350 pmol/min/μg under defined conditions .

The recombinant enzyme is supplied as a filtered solution in Tris and NaCl and should be stored at -20 to -70°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles to preserve the enzyme’s activity .