CISH polyclonal antibody

Src homology (SH2) domains are noncatalytic sequences that are conserved among a number of cytoplasmic signaling proteins. These signaling proteins are directly regulated by receptor tyrosine kinases and control the activation of mitogenic signal transduction pathways by such receptors (1-3). For instance, ligand-induced activation of the EGF and PDGF receptors induces dimerization, triggers receptor autophosphorylation on tyrosine residues and results in the binding of a number of cytoplasmic SH2 domain proteins such as PLC-g1 (4,5), Ras GAP (6) and PI 3-kinase p85 (5) to the activated receptors (4,5). The Shc gene encodes proteins with a single SH2 domain but no identifiable catalytic domain. CIS, cytokine-inducible SH2-containing protein, is a 267 amino acid protein with a single 96 amino acid SH2 domain that associates the tyrosine-phosphorylated beta chain of the IL-3 receptor with the tyrosine-phosphorylated Epo receptor (7). CIS was initially described as an immediate early cytokine-responsive gene and appears to be a unique regulator of cytokine signaling (7).