TPST1 Human

Tyrosine O-sulfation is a significant post-translational modification found in all multicellular organisms. It is essential for the proper functioning of various proteins, including those involved in cell signaling, adhesion, and immune response . Over 60 proteins have been identified to undergo tyrosine sulfation, and this modification is critical for their biological activity .

For instance, the sulfation of tyrosine residues in the leukocyte adhesion molecule P-selectin glycoprotein ligand 1 (PSGL-1) is necessary for its binding to P-selectin on activated endothelium . Additionally, the sulfation of chemokine receptors CCR5 and CXCR4 facilitates the entry of HIV-1 into target cells .

TPST1 is one of the two tyrosylprotein sulfotransferases found in the human genome, both of which have overlapping substrate specificities . TPST1 is widely expressed in all major tissues and is responsible for catalyzing the sulfation reaction of protein tyrosines . The enzyme’s activity is measured by its ability to transfer sulfate from PAPS to specific peptides, such as the PSGL-1 peptide .

Recombinant human TPST1 is produced using advanced biotechnological methods. It is typically expressed in a mouse myeloma cell line (NS0) and purified to achieve high purity levels, often exceeding 95% . The recombinant protein is supplied as a filtered solution in Tris and NaCl and is used in various research applications, including cell culture and enzyme assays .

Recombinant TPST1 is utilized in research to study the mechanisms of tyrosine sulfation and its impact on protein function. It is also used to investigate the role of sulfated proteins in various biological processes and diseases. For example, TPST1 knock-out mice have shown phenotypes of reduced body weight and increased post-implantation fetal death, highlighting the enzyme’s importance in development .