TPST1 Human, sf9

Tyrosylprotein Sulfotransferase 1 (TPST1) is an enzyme that plays a crucial role in the post-translational modification of proteins. Specifically, it catalyzes the sulfation of tyrosine residues within polypeptides, a process essential for various biological functions. TPST1 belongs to the protein sulfotransferase family and is involved in the formation of tyrosine O-sulfate ester groups .

The recombinant form of TPST1 is produced in Sf9 insect cells using the baculovirus expression system. This method allows for the production of a single, glycosylated polypeptide chain containing 354 amino acids (from 26 to 370 a.a.) with a molecular mass of approximately 40.6 kDa . The recombinant TPST1 is expressed with a 6-amino acid His tag at the C-terminus, which facilitates its purification through chromatographic techniques .

TPST1 is a membrane-bound enzyme localized in the Golgi apparatus. It utilizes 3’-phosphoadenosine-5’-phosphosulfate (PAPS) as the sulfonate donor and binds to proteins with target tyrosine residues to form the tyrosine O-sulfate ester group . The enzyme’s activity is crucial for various biological processes, including the inflammatory response .

The recombinant TPST1 protein is typically supplied as a sterile, filtered colorless solution. It is formulated in phosphate-buffered saline (PBS) with 10% glycerol to enhance its stability . For short-term storage, the protein can be kept at 4°C if used within 2-4 weeks. For long-term storage, it is recommended to store the protein at -20°C, with the addition of a carrier protein such as human serum albumin (HSA) or bovine serum albumin (BSA) to prevent multiple freeze-thaw cycles .

Recombinant TPST1 is widely used in biochemical and pharmaceutical research to study the sulfation of tyrosine residues and its implications in various biological processes. Its high purity and specific activity make it a valuable tool for investigating the role of tyrosine sulfation in protein function and signaling pathways .