Cloning, Fusion Expression And Purification Of Spap2 Domain Gene

In the quantities of regulation mechanisms of cell signal transduction, the phosphorylation and dephosphorylation of proteins are of importance. Especially, phosphorylation of specific cellular proteins on tyrosyl residues is one of the most fundamental regulatory mechanisms in signal transduction that dictates cell-cell communication, cell growth and proliferation, regulation of cell cycle and differentiation, tumorogenesis and tumor metastasis, nero tranmission, Angiogenesis, embryogeny, and kinds of hereditary and non-hereditary diseases. The research of protein tyrosine phophorylation has been hot spot in the field of biological science.SPAP2 is an intramembrane protein of immune receptor families containing both ITIMs and ITAMs. The extracellular portion of SPAP2 contains six immunoglobulin-like domains and its intracellular segment has two immunoreceptor tyrosine-based activation motifs (ITAMs) and two immunoreceptor tyrosine-based inhibition motifs (ITIMs). The SPAP2 gene contains 16 exons and is localized at human chromosome 1q21. A full-length cDNA of SPAP2 encodes a protein of 734 amino acid residues, intracellular segment of which has 137 amino acid residues. When stimulated and activated by signals fome outside , the tyrosyl residues of intracellular segment embedded in the two ITIM and two ITAM are phosphorylated, which induce SH2-domain containing PTP and PTK are translocalized from cytoplasm to membrane and bound to the...