Recombinant Rabbit Interleukin-2 (IL2) is expressed in E. coli and includes an N-terminal 6xHis tag that makes purification straightforward. The protein represents the complete mature form, covering amino acids 21 to 153. This product reaches purity levels above 90% when verified by SDS-PAGE, which appears to ensure consistent performance in research settings. It's designed strictly for research use and should not be considered for diagnostic or therapeutic applications.
Interleukin-2 (IL2) stands as a crucial cytokine within the immune system. Its primary function involves activating and promoting T cell proliferation. The protein plays what seems to be a significant role in regulating immune responses and acts as a key element in immune signaling pathways. Given IL2's central importance in immune research, it likely represents a valuable tool for studies focused on immune regulation and related therapeutic developments.
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. Rabbit-Specific Immunological Research
This recombinant rabbit IL-2 may serve as a species-matched cytokine for examining T-cell proliferation and activation in rabbit-derived cell cultures or primary lymphocytes. The protein offers a standardized reagent for investigating rabbit immune responses in vitro, especially for research involving rabbit models of autoimmune diseases or transplantation studies. The N-terminal 6xHis tag makes purification and immobilization relatively simple in experimental setups that require controlled cytokine presentation.
2. Comparative Cytokine Biology Studies
Rabbit IL-2 protein appears to enable comparative analysis of interleukin-2 function across different mammalian species when researchers pair it with human, mouse, or other IL-2 orthologs. Scientists can examine what may be species-specific differences in receptor binding affinity, signaling pathway activation, or downstream cellular responses through standardized in vitro assays. This application seems particularly valuable for understanding evolutionary conservation of cytokine functions and species-specific immune mechanisms.
3. Anti-IL-2 Antibody Development and Validation
The recombinant protein functions as an antigen for generating rabbit IL-2-specific antibodies or for validating existing antibodies in research applications. High purity levels (>90%) and the defined sequence (aa 21-153) suggest it's well-suited for immunization protocols, ELISA development, or Western blot validation studies. The His-tag likely makes protein immobilization on surfaces more manageable for antibody screening assays and binding kinetics studies.
4. Protein-Protein Interaction Studies
His-tagged rabbit IL-2 can be applied in pull-down assays to identify and characterize IL-2 receptor components or other binding partners from rabbit cell lysates. The tag appears to enable efficient immobilization on nickel-affinity matrices for capturing interacting proteins, which researchers can then analyze by mass spectrometry or immunoblotting. This approach may prove useful for mapping IL-2 signaling complexes and identifying what could be novel regulatory proteins in rabbit immune cells.
5. Cell Culture Supplementation for Rabbit Cell Lines
This recombinant protein provides what appears to be a defined, consistent source of IL-2 for maintaining rabbit T-cell lines or primary lymphocyte cultures in research settings. The E. coli expression system seems to ensure batch-to-batch consistency compared to cell culture-derived cytokines, while the species-matched origin likely ensures optimal biological compatibility with rabbit cells. Standardized protein concentration and purity may help create reproducible experimental conditions across different research laboratories.
