A recombinant fragment of human IL5 protein corresponding to the mature protein sequence was used as the immunogen for the Interleukin 5 antibody.
Interleukin-5, or IL-5, was originally discovered as a soluble T cell-derived factor, called T cell-replacing factor (TRF), that induced T cell-depleted activated B cells to secrete immunoglobulin. Native IL-5 is a disulfide-linked homodimer. IL-5 is initially synthesized as a precursor with a 19 amino acid signal peptide which is cleaved to form a 112 amino acid mature protein. Murine and human IL-5 exhibit 70% sequence identity at the amino acid level. IL-5 exerts its biological activity through the IL-5 receptor (IL-5R), which is composed of at least two chains: an chain that binds IL-5 with low affinity and a chain that does not bind IL-5, but together with the IL-5 a chain, constitutes the high affinity IL-5 receptor. The chain is common to the IL-3, IL-5 and GM-CSF receptors and has been shown to signal through the JAK/Stat pathway.
