hIL4-PE4E

**hIL4-PE4E** is a recombinant fusion protein consisting of human interleukin 4 (hIL4) genetically fused to a mutated form of Pseudomonas exotoxin A (PE4E), which lacks native receptor binding activity. This chimeric cytotoxin is designed to selectively target and kill cells expressing the interleukin-4 receptor (IL4R), which is overexpressed in a variety of hematological malignancies and solid tumors. The mechanism of action involves hIL4-mediated binding to IL4R on the target cell surface, followed by internalization of the toxin and subsequent inhibition of protein synthesis, resulting in cell death. The construct was developed and studied at the National Cancer Institute (NCI), National Institutes of Health (NIH), primarily as an experimental anti-cancer agent[1].

Other names

human interleukin-4–pseudomonas exotoxin A (mutant PE4E) fusion proteinhIL4-PE chimeric toxinhIL-4-PE chimeric toxinhIL 4-PE chimeric toxin