SIRP alpha/CD172a Protein, Human (Biotinylated, HEK293, His-Avi)

SIRP alpha V4/CD172a Protein, an immunoglobulin-like cell surface receptor for CD47, acts as a docking protein that facilitates the translocation of PTPN6, PTPN11, and other binding partners from the cytosol to the plasma membrane. This receptor contributes to diverse cellular processes, including supporting the adhesion of cerebellar neurons, promoting neurite outgrowth, and facilitating glial cell attachment. With a potential role in intracellular signaling during synaptogenesis and synaptic function, SIRP alpha V4/CD172a also engages in negative regulation of receptor tyrosine kinase-coupled responses triggered by cell adhesion, growth factors, or insulin. Furthermore, it mediates the negative modulation of phagocytosis, mast cell activation, and dendritic cell activation. Notably, CD47 binding prevents the maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. SIRP alpha V4/CD172a plays a significant role in antiviral immunity, limiting new world arenavirus infection by decreasing virus internalization. As a receptor for THBS1, it participates in ROS signaling in non-phagocytic cells upon interaction with THBS1, stimulating NADPH oxidase-derived ROS production. The receptor engages in various protein interactions, including binding to PTPN11, GRB2, FGR, JAK2, SCAP1, SCAP2, FYB1, PTK2B, and TRIM2.