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Protein tyrosine phosphatases (PTPases) SHP-1 and SHP-2 are critical regulators in the intracellular signaling pathways that result in cell responses such as mitosis, differentiation, migration, survival, transformation or death. SHP-2 is a signal transducer for several receptor tyrosine kinases and cytokine receptors. A novel SHP-2 associated glycoprotein was recently cloned from human, rat, mouse and cattle by several labs and was designated SIRPa (1), SHPS-1 (2,3), MyD-1 (4), BIT (5,6) and p84 (7). SIRPa is a new gene family containing at least fifteen members. SIRPa is a substrate of many activated tyrosine kinases such as insulin receptor, EGFR, PDGFR and src, and a specific docking protein for SHP-2 (1,2,5,8). SIRPa has regulatory effects on cellular responses induced by serum, growth factors, insulin, oncogenes, growth hormones and cell adhesion and plays a general role in different physiological and pathological processes (1,2,5,8).