TPST2 Human, sf9

TPST2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 361 amino acids, specifically from the 26th to the 377th amino acid. The molecular mass of this recombinant protein is approximately 40.4 kDa, although it migrates at 40-57 kDa on SDS-PAGE under reducing conditions . The enzyme is expressed with a 6 amino acid His tag at the C-terminus, which facilitates its purification through proprietary chromatographic techniques .

The primary function of TPST2 is to catalyze the transfer of a sulfate group from the donor molecule 3’-phosphoadenosine-5’-phosphosulfate (PAPS) to the hydroxyl group of tyrosine residues in target proteins. This sulfation process is critical for the biological activity, stability, and interaction of various proteins. Sulfated tyrosine residues are often found in proteins involved in cell signaling, adhesion, and extracellular matrix interactions.

Recombinant TPST2, such as the one produced in Sf9 cells, is widely used in biochemical and pharmaceutical research. It allows scientists to study the sulfation process in detail and understand its implications in health and disease. The availability of human recombinant TPST2 enables the exploration of its role in various physiological and pathological conditions, including cancer, inflammation, and infectious diseases.

The production of TPST2 in Sf9 Baculovirus cells involves the use of a baculovirus expression system, which is known for its ability to produce high yields of recombinant proteins with proper post-translational modifications. The glycosylation of TPST2 is essential for its stability and activity. The purification process typically involves affinity chromatography, taking advantage of the His tag to isolate the enzyme from other cellular proteins.