Recombinant Human IL-5 R alpha Protein

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Interleukin-5 Receptor alpha (IL-5 R alpha ), also known as CD125, is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology (1 - 3). Mature human IL-5 R alpha consists of a 322 amino acid (aa) extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain (4, 5). Within the ECD, human IL-5 R alpha shares 71% aa sequence identity with mouse and rat IL-5 R alpha . Alternate splicing of human IL-5 R alpha generates soluble secreted forms which function as IL-5 antagonists (5 - 7). The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL‑5 R alpha and the transmembrane common beta chain ( beta c/CD131) which is shared with the receptor complexes for IL-3 and GM-CSF (4). IL-5 R alpha binds IL-5 at low affinity and then associates with preformed beta c oligomers to form the signaling-competent receptor complex (8). IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the upregulation of transmembrane IL-5 R alpha followed by eosinophilic differentiation and activation (9 - 11). IL‑5 R alpha also promotes the differentiation of basophils and B cells (12, 13). Exposure of mature eosinophils to IL-5 attenuates their IL-5 responsiveness by inducing the downregulation of surface IL-5 R alpha and increased production of soluble IL-5 R alpha (14, 15). Elevated production of IL-5 at sites of allergic inflammation induces eosinophilia and exacerbation of immune cell infiltration, tissue damage, and remodeling (2, 3).

Array 253-5R

• IL-5R alpha/CD125 Antibodies
• IL-5R alpha/CD125 Lysates
• IL-5R alpha/CD125 Proteins and Enzymes