Recombinant Rhesus Macaque Interleukin-4 protein (IL4) is produced in E. coli with the full-length mature protein expressed from amino acids 25 to 153. This product is tag-free and achieves a high purity level exceeding 96%, confirmed by SDS-PAGE analysis. The protein demonstrates full biological activity, with an ED50 of less than 1.0 ng/ml in a cell proliferation assay using human TF-1 cells. Endotoxin levels remain below 1.0 EU/µg, determined by the LAL method.
Interleukin-4 (IL-4) appears to be a key cytokine involved in immune response regulation, primarily influencing the differentiation of naive helper T cells to Th2 cells. It plays what seems to be a critical role in promoting B-cell differentiation and antibody production. IL-4 is likely integral to understanding allergic inflammatory responses and has significant implications in research focused on immune modulation and related disorders.
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 in Primate Cell Models
This biologically active rhesus macaque IL-4 protein can stimulate cell proliferation in primate-derived cell lines and primary cells for research purposes. Given its demonstrated activity on human TF-1 cells with an ED50 of less than 1.0 ng/ml, it may provide a reliable tool for dose-response studies examining IL-4-mediated cellular responses. The high purity (>96%) and low endotoxin levels make it suitable for sensitive cell culture experiments where contamination could confound results. Researchers can apply this protein to investigate species-specific differences in IL-4 signaling between human and non-human primate systems.
2. Cytokine Signaling Pathway Analysis
The recombinant protein serves as what appears to be a valuable reagent for studying IL-4 receptor binding and downstream signaling cascades in primate research models. Its biological activity allows researchers to examine STAT6 phosphorylation, JAK activation, and other IL-4-dependent signaling events in various cell types. The tag-free nature of the protein eliminates potential interference from fusion tags that might affect receptor binding or signaling kinetics. This application seems particularly relevant for comparative immunology studies investigating evolutionary conservation of cytokine signaling mechanisms.
3. Antibody Development and Validation Studies
This highly pure rhesus macaque IL-4 protein can work as an antigen for generating species-specific antibodies or as a standard for validating existing anti-IL-4 antibodies. The mature protein sequence (25-153aa) represents the naturally occurring form, making it ideal for developing antibodies that recognize native IL-4 in rhesus macaque samples. Researchers can apply this protein in ELISA development, Western blot validation, and other immunoassays requiring a reliable IL-4 standard. The low endotoxin content ensures minimal interference in antibody production protocols.
4. Comparative Cytokine Function Studies
The biologically active rhesus macaque IL-4 enables direct comparison of cytokine function between human and non-human primate systems in controlled laboratory settings. Researchers can perform parallel experiments using this protein alongside human IL-4 to assess cross-species reactivity and functional differences. The established activity profile on human TF-1 cells provides a baseline for comparing responses across different cell types and species. This application may support translational research efforts where rhesus macaque models are used to study human immunological processes.
5. Protein-Protein Interaction Studies
This recombinant IL-4 protein can work in biochemical assays to study its interactions with IL-4 receptors, binding proteins, or other molecular partners. The high purity and biological activity suggest reliable results in surface plasmon resonance, bio-layer interferometry, or other binding affinity measurements. Researchers can investigate the kinetics and thermodynamics of IL-4 interactions in primate systems, contributing to understanding of cytokine-receptor biology. The tag-free format appears particularly advantageous for these applications as it eliminates potential steric hindrance or artificial binding interactions.
