Interleukin-13 receptor subunit alpha-2 (345-353)

Interleukin-13 receptor subunit alpha-2 (345-353) is a synthetic peptide fragment derived from the C-terminal region of the IL-13Rα2 protein, a high-affinity receptor for the cytokine interleukin-13. This peptide is of significant interest within immunology and molecular biology research due to its role in modulating IL-13 signaling pathways, which are implicated in various immune responses and pathological processes. As a defined sequence corresponding to residues 345 to 353 of the IL-13Rα2 protein, it provides a valuable molecular tool for dissecting protein-protein interactions, mapping functional domains, and developing targeted assays in the context of cytokine biology.

Epitope mapping: Researchers utilize this peptide fragment to identify and characterize antibody binding sites within the IL-13Rα2 protein. By employing the 345-353 sequence in immunoassays or as a substrate in peptide array platforms, it is possible to delineate specific linear epitopes recognized by monoclonal or polyclonal antibodies. This approach is essential for the development of high-affinity antibodies for research or diagnostic use, as well as for understanding immune recognition mechanisms at the molecular level.

Receptor-ligand interaction studies: The defined sequence of the 345-353 region enables detailed investigation of the molecular interactions between IL-13Rα2 and its ligands or associated signaling partners. By incorporating the peptide into binding assays or competitive inhibition experiments, researchers can probe the structural determinants critical for cytokine-receptor engagement and downstream signaling modulation. These studies contribute to the broader understanding of cytokine receptor biology and inform the rational design of molecular probes or inhibitors.

Peptide-based assay development: The synthetic peptide serves as a standard or calibrator in a variety of biochemical and immunological assays, including enzyme-linked immunosorbent assays (ELISA) and surface plasmon resonance (SPR) analyses. Its use facilitates the quantification of specific antibody or protein interactions, validation of assay specificity, and optimization of detection protocols. The availability of a well-characterized peptide sequence enhances assay reproducibility and supports the development of robust analytical platforms for IL-13Rα2 research.

Structure-function analysis: Incorporating the 345-353 peptide into structure-activity relationship (SAR) studies allows scientists to assess the functional relevance of this region within the full-length receptor. Through techniques such as alanine scanning or peptide mutagenesis, the contribution of individual amino acids to receptor conformation, stability, or interaction with binding partners can be systematically evaluated. These insights are instrumental for elucidating the mechanistic basis of IL-13Rα2 function and may guide future protein engineering efforts.

Immunogenicity assessment: The peptide fragment is also employed in studies evaluating T-cell or B-cell responses against specific regions of the IL-13Rα2 protein. By presenting the 345-353 sequence in ex vivo or in vitro assays, researchers can monitor immune cell activation, cytokine production, or antibody generation in response to this epitope. Such analyses are valuable for understanding immune surveillance mechanisms, developing immunological reagents, or characterizing host responses to recombinant proteins.

1. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

2. Olfactory receptor based piezoelectric biosensors for detection of alcohols related to food safety applications

3. Identification, Localization in the Central Nervous System and Novel Myostimulatory Effect of Allatostatins in Tenebrio molitor Beetle

4. High fat diet and GLP-1 drugs induce pancreatic injury in mice

5. P-selectin and Complement’s Role in a Neonatal Model of Germinal Matrix Hemorrhage-Induced Secondary Injury