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The t(11;22)(p13;q12) chromosomal translocation is detected in most cases of Ewing's sarcoma, a tumor of bone and soft tissue. This genetic alteration results in the expression of a chimeric protein termed EWS/FLI. The EWS/FLI protein contains six potential phosphorylation sites, one of which is highly conserved and is conserved in EWS of the t(21;22)(q22;q12) variant of t(22q12) Ewing's sarcoma, in which the fusions are different. In this study, we have characterized the cDNA for EWS and have cloned it into pET23b to express the GST fusion protein. In vitro kinase assays show that the conserved serine in EWS can be phosphorylated in vitro. We also demonstrate that the GST fusion protein can be used to identify the presence of antibodies reactive with the phosphorylated 65-kDa form of EWS. Anti-EWS antibodies from patients with Ewing's sarcoma react with a 65-kDa protein in blots of whole cell lysates or of cell extracts that contain the 65-kDa form of EWS, but not in blots of lysates from RK13 (control), which do not contain the fusion protein. No reactivity is detected with anti-EWS antibodies in blotting patterns from cells that do not contain EWS. The 65-kDa protein is detected only when the blot is incubated with sera of 0b46394aab
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