IL13RA1 Human
Description
IL13RA1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
IL13RA1 is a type I membrane protein that belongs to the hemopoietin receptor family. The human IL13RA1 gene encodes a precursor protein consisting of 427 amino acids. This precursor includes a 21 amino acid signal peptide, a 324 amino acid extracellular domain, a 23 amino acid transmembrane region, and a 59 amino acid cytoplasmic tail . The extracellular domain of IL13RA1 is closely related to that of IL13RA2, another subunit of the IL-13 receptor.
IL13RA1 forms a receptor complex with the IL-4 receptor alpha (IL4RA) subunit, which is shared by both IL-13 and IL-4 receptors . This complex is essential for binding IL-13 with high affinity and mediating its biological effects. IL13RA1 serves as the primary IL-13 binding subunit and is involved in the activation of downstream signaling pathways, including the JAK-STAT pathway. Specifically, it has been shown to bind tyrosine kinase TYK2, leading to the activation of JAK1, STAT3, and STAT6 .
Recombinant human IL13RA1 is produced using various expression systems, such as HEK293 cells. The recombinant protein typically includes a polyhistidine tag (His tag) for purification purposes . The recombinant IL13RA1 protein consists of 333 amino acids and has a predicted molecular mass of approximately 38.3 kDa. Due to glycosylation, the apparent molecular mass of the recombinant protein is around 55-65 kDa when analyzed by SDS-PAGE under reducing conditions .
The recombinant IL13RA1 protein is often used in research to study its binding affinity with IL-13 and to investigate the signaling mechanisms mediated by the IL-13 receptor complex. For example, it has been shown that recombinant IL13RA1 can bind IL-13 with an affinity constant of 10.20 nM in a surface plasmon resonance (SPR) assay .
Understanding the structure and function of IL13RA1 is crucial for developing therapeutic strategies targeting IL-13 mediated diseases, such as asthma, allergies, and certain autoimmune disorders. By studying the recombinant form of IL13RA1, researchers can gain insights into the molecular mechanisms underlying IL-13 signaling and identify potential targets for drug development.
