Sulfotyrosine Antibody, Clone 12B11: Biotin

Tyrosine sulfation is a widespread and functionally significant post-translational modification catalyzed by tyrosylprotein sulfotransferases (TPSTs) . This process results in the formation of sulfotyrosine residues, which play a critical role in modulating protein–protein interactions across diverse biological systems. Sulfotyrosines are essential for high-affinity binding in several well-characterized molecular interactions, including those between hirudin and thrombin, P-selectin glycoprotein ligand-1 and P-selectin, and von Willebrand factor and factor VIII. Emerging evidence suggests that tyrosine sulfation may also influence key pathways in the nervous system, with implications for neurodegenerative disease research. Sulfated tyrosine residues on chemokine receptors and other membrane proteins are known to regulate cellular signaling, immune responses, and pathogen entry—mechanisms that are increasingly recognized as contributors to neuroinflammation and neurodegeneration. Furthermore, the requirement of tyrosine sulfation for viral and parasitic entry into host cells highlights its potential relevance in neurotropic infections and associated neuropathologies. As the neuroscience field continues to explore the epigenetic and post-translational landscapes of brain function and dysfunction, sulfotyrosine is gaining attention as a modulator of neuronal communication, immune surveillance, and disease progression. Understanding its role could open new avenues for therapeutic intervention in neurodegenerative disorders.

A 1:1000 dilution of SMC-522 was sufficient for detection of Sulfotyrosine in 0.5 µg of Sulfotyrosine conjugated to BSA by ECL immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary Antibody.