Tyrosine sulfation antibodies are the most common tools for the detection and study of tyrosine-sulfated proteins. Creative Biolabs provides the global customers with high-efficiency and tyrosine sulfation-specific antibody production service based on our phage display platform and High-Affi™ technology.
Tyrosine sulfation is a common post-translational modification that a tyrosine residue of proteins is transferred of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate by the tyrosylprotein sulfotransferase (TPST) in the trans-Golgi apparatus. Sulfation, first discovered by Bettelheim in 1954, was found from animals to plants but not in yeasts or prokaryotes. The process of tyrosine sulfation is irreversible in vivo and tyrosine O-sulfate is very stable and difficult to be degraded by mammalian sulfatases. Extracellular parts of membrane proteins and secreted proteins that pass through the Golgi apparatus may be sulfated. Currently, the proteins are known to undergo tyrosine sulfation include extracellular matrix proteins, adhesion molecules, G-protein-coupled receptors, hormones, coagulation factors, and serine protease inhibitors.
Recent studies have shown that nitrotyrosine occurs sulfation in cells under oxidative/nitrative stress, catalyzed by SULT1A3. Numerous physiological processes are mediated by tyrosine sulfation such as protein-protein interactions involved in leukocyte adhesion and receptor-mediated signaling of P-selectin glycoprotein ligand-1 with P-selectin. Tyrosine sulfation is also involved in the entry of several parasites and viruses. As an example, when HIV virus is entering into host cells, it is essential to the HIV-1 co-receptor CCR5 to get tyrosine sulfation. Tyrosine sulfation is also found on the Duffy antigen/receptor for chemokines, and this is essential to erythrocyte invasion of the malaria parasite Plasmodium vivax. However, disfunction of tyrosine sulfation links to diverse diseases. TPST genes knock-out in mice effects on the growth, such as body weight, fecundity, and postnatal viability. Removal of sulfated tyrosine residues decreases the binding affinity of the ligand to its corresponding receptor, such as PSGL-1, CD44v5, CCR5, and CXCR4, leading to a variety of autoimmune diseases.
Fig. 1 The tyrosylprotein sulfotransferase reaction. (Moore K. L. 2003)
Fig. 2 Protein tyrosine sulfation (PTS) and its biological path. (Yang Y.S., Wang C.C., Chen B.H., et al. 2015)
Protein tyrosine sulfation involved in many cellular events, making their detection vital for the study of various human diseases. Creative Biolabs is one of the most professional companies in developing high-quality monoclonal antibodies of various species based on advanced technologies. Our experienced scientists will tailor the most appropriate methods and 100% guaranteed service for customers.
In addition to the tyrosine sulfation-specific antibody, Creative Biolabs also provides a comprehensive list of PTM-specific antibody production services of your choice.
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