Human IL-13 R alpha1 Biotinylated Antibody

Two type 1 membrane proteins belonging to the hemopoietin receptor family have been cloned and shown to bind IL-13 with differing affinities. The lower affinity IL-13 binding protein, previously designated IL-13 R alpha, IL-13 R alpha' or NR4, is now referred to as IL-13 R alpha1. The high-affinity IL-13 binding protein, previously also designated IL-13 R or IL-13 R alpha', is now referred to as IL-13 R alpha2.

The human IL-13 R alpha1 was originally cloned based on sequence homology to the mouse IL-13 R alpha1. The IL-13 R alpha1 cDNA encodes a 427 amino acid (aa) residue precursor protein with a putative 21 aa residue signal peptide, a 324 aa residue extracellular domain, a 23 aa residue transmembrane region, and a 59 aa residue cytoplasmic tail. Human and mouse IL-13 R alpha1 share 76% aa sequence identity. The extracellular domain of IL-13 R alpha1 is also closely related to that of IL‑13 R alpha2. IL‑13 R alpha1 has been shown to combine with the IL-4 R alpha to form a high-affinity receptor complex capable of transducing an IL-13-dependent proliferative signal. The role of IL-13 R alpha2 in IL-13 signaling remains to be elucidated.