Recombinant Macaca mulatta Interleukin-10 (IL10) is expressed in E. coli and comprises the full length of the mature protein, covering the amino acid region 19-178. The protein features an N-terminal 6xHis-B2M tag to facilitate purification and detection. It achieves a purity level greater than 90% as determined by SDS-PAGE, ensuring a high-quality product suitable for research applications. This product is intended for research use only.
Interleukin-10 (IL10) appears to be a cytokine with a crucial role in controlling immune responses. It's known for its anti-inflammatory properties, helping to rein in immune reactions and prevent damage to the host during infections. IL10 is involved in various signaling pathways and can influence how immune cells like macrophages and T cells function. Its importance in immunological research makes it a valuable tool for studying immune modulation.
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.
Macaca mulatta IL-10 is a cytokine that functions as an anti-inflammatory homodimer, requiring precise folding and disulfide bond formation for biological activity. The E. coli expression system cannot perform the necessary eukaryotic post-translational modifications and may not facilitate correct disulfide bonding or dimerization. The unusual B2M (beta-2-microglobulin) fusion tag is particularly problematic as it may cause improper folding or steric hindrance of IL-10's receptor-binding domains. Therefore, this recombinant protein is highly unlikely to be correctly folded or functionally active.
1. Antibody Development and Validation Studies
This recombinant IL-10 protein serves as a suitable immunogen for generating antibodies against linear epitopes of rhesus macaque IL-10. The full-length mature sequence ensures comprehensive epitope coverage. However, antibodies produced against this misfolded, bacterially expressed protein may not efficiently recognize conformational epitopes on the native, properly folded, and dimerized IL-10 in biological samples.
2. Biochemical Characterization and Stability Studies
This application is valuable for assessing the physical properties of this specific protein preparation. Techniques like size-exclusion chromatography can evaluate oligomeric state (likely misfolded monomers/aggregates rather than functional dimers), while circular dichroism can analyze secondary structure content and thermal stability. These studies provide essential quality control data about the protein itself, regardless of functional status.
Final Recommendation & Action Plan
This recombinant IL-10 is compromised by both the E. coli expression system and the problematic B2M fusion tag, making it unsuitable for functional studies. The recommended approach is to prioritize Application 2 (Biochemical Characterization) to understand the protein's physical properties, then proceed cautiously with Application 1 (Antibody Development) for linear epitope antibodies. Protein-receptor interactions require a precise three-dimensional conformation that this misfolded, tagged protein cannot provide. Comparative functional studies with IL-10 from other species would be invalid due to the protein's likely misfolded state and presence of the artificial B2M tag.
