IL-13RA1 His Tag Protein, Mouse

Interleukin 13 receptor, alpha 1 (IL13RA1), also known as NR4 or CD213A1 (cluster of differentiation 213A1), is encoded by the IL13RA1 cDNA. This cDNA specifies a precursor protein consisting of 427 amino acids (aa), which includes a putative 21 aa signal peptide, a 324 aa extracellular domain, a 23 aa transmembrane region, and a 59 aa cytoplasmic tail.
IL13RA1 is a critical subunit of the interleukin 13 receptor complex. It pairs with the alpha subunit of the interleukin 4 receptor (IL4Rα), a component shared by both IL13 and IL4 receptor complexes. IL13RA1 serves as the primary IL13-binding subunit for the IL13 receptor and may also contribute to the structure of IL4 receptors. This protein is known to interact with the tyrosine kinase TYK2, potentially mediating signaling cascades that activate JAK1, STAT3, and STAT6 in response to IL13 and IL4. It exhibits low affinity binding to interleukin-13 (IL13) and, in conjunction with IL4RA, forms a functional receptor for IL13. Additionally, IL13RA1 acts as an alternative accessory protein to the common cytokine receptor gamma chain (IL2RG) in IL4 signaling, although it cannot enhance interleukin-2 (IL2) binding activity as IL2RG does.
In pancreatic cancer cells, IL-4 and IL-13 primarily exert their effects through their receptor heterodimers, IL-4Rα and IL13RA1, also known as type II IL-4R. They activate signaling pathways including STAT3/6, IRS-ERK/PI3K-Akt, and mTOR.