Recombinant human SIRP alpha/CD172a protein

SIRP alpha is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRP alpha interacts with a broadly expressed transmembrane protein CD47. This interaction negatively controls effector function of innate immune cells such as host cell phagocytosis. This protein can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and serve as substrates of PTPs. It was found to participate in signal transduction mediated by various growth factor receptors. Recombinant human SIRP alpha, fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques.