Recombinant Human Interleukin-13 protein (IL13) is produced in an E. coli expression system and comes in a tag-free format. The protein covers the full length of the mature protein, from amino acids 35 to 146. SDS-PAGE analysis confirms a high purity level exceeding 97%. The protein maintains full biological activity, showing an ED50 of less than 1 ng/ml in cell proliferation assays with human TF-1 cells and specific activity greater than 1.0 × 10^6 IU/mg. Endotoxin levels remain tightly controlled at less than 1.0 EU/µg, as measured by the LAL method.
Interleukin-13 (IL13) is a cytokine that T helper 2 (Th2) cells primarily produce. This protein appears to play a crucial role in immune system regulation, particularly in controlling inflammatory responses during allergic reactions and asthma. IL13 is likely involved in pathways that influence immunoglobulin E (IgE) production and may promote B cell differentiation. Its importance in research stems from its involvement in immune responses and potential therapeutic applications in conditions where excessive inflammation occurs.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Cell Proliferation and Viability Assays
This recombinant IL-13 protein can stimulate cell proliferation in IL-13-responsive cell lines for cytokine signaling pathway research. With its demonstrated biological activity showing an ED50 of less than 1 ng/ml in TF-1 cell proliferation assays, it works as a reliable positive control or experimental stimulus. Researchers might use this protein to examine dose-response relationships, fine-tune culture conditions, or explore how IL-13 affects different hematopoietic and immune cell types in laboratory settings.
2. Cytokine Receptor Binding Studies
The biologically active IL-13 protein works well in receptor binding assays to study interactions between IL-13 and its specific receptors, including IL-13Rα1 and IL-13Rα2. Surface plasmon resonance, competitive binding assays, or flow cytometry-based binding studies can incorporate this protein to measure binding kinetics, determine affinity constants, and assess receptor expression levels across various cell types. The high purity (>97%) and tag-free design make it suitable for precise binding measurements without interference from contaminants or added tags.
3. Signal Transduction Pathway Analysis
This recombinant IL-13 can act as a stimulus to explore downstream signaling cascades that activate when IL-13 engages its receptors, particularly the JAK-STAT pathway. Researchers may use this protein to examine phosphorylation events, transcription factor activation, and gene expression changes in target cells through Western blotting, immunofluorescence, or qRT-PCR techniques. The confirmed biological activity suggests reliable activation of IL-13-mediated signaling pathways for mechanistic studies.
4. Antibody Development and Validation
The high-purity, tag-free IL-13 protein can serve as an immunogen for creating research antibodies or as a standard for testing existing anti-IL-13 antibodies. Its biological activity provides a functional readout in neutralization assays to evaluate antibody effectiveness. This protein also works in ELISA development, Western blot validation, or immunoprecipitation experiments to determine antibody specificity and sensitivity.
5. Protein-Protein Interaction Studies
This recombinant IL-13 can be used in co-immunoprecipitation, pull-down assays, or yeast two-hybrid systems to identify and study proteins that interact with IL-13 beyond its known receptors. The tag-free design eliminates potential artifacts from fusion tags, while the high purity helps ensure specific interactions. Researchers might investigate novel binding partners, examine protein complex formation, or validate predicted interactions from computational studies using this biologically active protein as bait or target.
