Anti-SPSB2 / SplA/Ryanodine receptor domain and SOCS box containing protein 2

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. SPSB2 antibody detects SplA/Ryanodine receptor domain and SOCS box containing protein 2, an adaptor molecule involved in ubiquitin-mediated proteasomal degradation. The UniProt recommended name is SplA/Ryanodine receptor domain and SOCS box containing protein 2 (SPSB2). This cytoplasmic protein interacts with substrate proteins through its SPRY domain and recruits E3 ubiquitin ligase complexes via its SOCS box, promoting targeted protein turnover.Functionally, SPSB2 antibody identifies a 293-amino-acid protein that regulates signaling through inducible nitric oxide synthase (iNOS), erythropoietin, and other cytokine-related pathways. SPSB2 binds iNOS, targeting it for proteasomal degradation, thereby controlling nitric oxide production and inflammatory responses. Through this mechanism, SPSB2 contributes to feedback inhibition in immune signaling and maintains cellular redox balance.The SPSB2 gene is located on chromosome 12q24.31 and encodes a member of the SPSB family, which includes SPSB1, SPSB3, and SPSB4. Each family member functions as an adaptor in ubiquitin ligase complexes, characterized by their conserved SPRY and SOCS domains. SPSB2 expression is high in macrophages, spleen, and liver, reflecting its role in immune regulation and metabolic processes.Pathologically, dysregulated SPSB2 activity affects nitric oxide signaling, contributing to inflammatory disorders, cancer progression, and metabolic stress. By promoting degradation of iNOS, SPSB2 helps terminate inflammatory responses and prevent tissue damage. Reduced SPSB2 levels may prolong nitric oxide signaling, leading to oxidative stress or chronic inflammation.SPSB2 antibody is suitable for western blotting, immunohistochemistry, and immunoprecipitation to study protein degradation mechanisms, immune signaling, and nitric oxide regulation. NSJ Bioreagents provides validated SPSB2 antibody reagents optimized for research in protein ubiquitination, cytokine signaling, and inflammation control.Structurally, SPSB2 contains an N-terminal SPRY domain mediating substrate recognition and a C-terminal SOCS box that binds elongin B/C, Cullin 5, and Rbx2 to assemble an E3 ligase complex. This modular configuration enables selective targeting of regulatory proteins for degradation, linking SPSB2 to diverse cellular pathways governing inflammation and metabolism.