CHST9
CHST9 (carbohydrate sulfotransferase 9) is a membrane-bound sulfotransferase of the sulfotransferase 2 family that transfers sulfate to N-acetylgalactosamine residues on glycans. It is also known as GALNAC4ST-2 or GALNAC-4-ST2. Browse Assay Genie's current range of CHST9 research reagents below, or read on for the biology behind the target.
CHST9 is a carbohydrate sulfotransferase that catalyses the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues. According to the NCBI Gene summary, this activity occurs on both N-glycans and O-glycans. UniProt annotates the enzyme as active against chondroitin but not against terminal beta-1,4-linked GalNAc, which helps define its substrate preference.
The protein encoded by the CHST9 gene belongs to the sulfotransferase 2 family and is localised to the Golgi membrane, where glycan modification takes place. UniProt also lists a secreted form. HGNC places it in the group of membrane-bound sulfotransferases. Alternatively spliced transcript variants have been described for this gene. The mouse ortholog is Chst9.
Sulfate groups on carbohydrates confer highly specific functions on glycoproteins, glycolipids and proteoglycans, and are described as critical for cell-cell interaction, signal transduction and embryonic development. CHST9 therefore contributes to a layer of glycan regulation that shapes how these molecules behave. The protein has also been named GALNAC4ST-2 and GALNAC-4-ST2, and the gene was previously named carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 9, reflecting its GalNAc 4-O-sulfation activity. Researchers studying CHST9 protein function often compare it with related carbohydrate sulfotransferases such as CHST13.
CHST9 adds sulfate to the 4-position of non-reducing GalNAc on N-glycans and O-glycans, making it a useful enzyme for studying glycan sulfation.
UniProt reports activity against chondroitin, linking CHST9 to the study of sulfated glycosaminoglycan and proteoglycan structure.
Carbohydrate sulfation is described as critical for cell-cell interaction and signal transduction, so CHST9 is relevant to glycan-dependent signalling.
Sulfate groups on carbohydrates are described as critical for embryonic development, placing sulfotransferases such as CHST9 within developmental glycobiology.
CHST9 catalyses the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine residues in N-glycans and O-glycans. UniProt describes it as active against chondroitin but not against terminal beta-1,4-linked GalNAc. It acts in the Golgi membrane.
CHST9 is also called GALNAC4ST-2 and GALNAC-4-ST2. Its former HGNC name was carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 9. The current full name is carbohydrate sulfotransferase 9. Alternatively spliced transcript variants have been described for the gene.
A mouse ortholog, Chst9, is recorded for the human gene. CHST9 belongs to the sulfotransferase 2 family. For any research product, check the datasheet of any product for its validated reactivity before use in a given species.
Other carbohydrate sulfotransferases and glycan-modifying enzymes related to CHST9 research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q7L1S5; product specifications from Assay Genie datasheets.