Recombinant Equine Interleukin-2 (rEqIL-2) is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain containing 129 amino acids. The recombinant form often includes a substitution of serine for cysteine at position 141 (Cys141Ser), resulting in a molecular mass of approximately 14.9 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity and biological activity .
IL-2/IL-2R signaling is essential for T cell proliferation and other fundamental immune functions. The receptor for IL-2 consists of three subunits: IL-2Rα (55 kDa), IL-2Rβ (75 kDa), and the common gamma chain (γc/IL-2Rγ, 64 kDa). These subunits are present on the cell surface in varying preformed complexes .
Recombinant equine IL-2 has been shown to augment proliferation in equine peripheral blood mononuclear cells (PBMCs) and enhance cellular proliferation. It significantly upregulates the transcription and secretion of various cytokines, including IFN-γ, TNF-α, IL-4, IL-10, and IL-12p35 .
Recombinant equine IL-2 is used in various research and clinical applications, particularly in immunology and veterinary medicine. It is utilized to study the immune response in horses and to develop treatments for equine diseases. The recombinant form allows for controlled studies and consistent results, making it a valuable tool in scientific research .