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MSA-hoIL2 is a recombinant fusion protein designed for preclinical oncology research, consisting of mouse serum albumin (MSA) fused to a human interleukin-2 (IL-2) variant. The IL-2 component, often referred to as 'hoIL2' (half-life optimized IL-2) or the 'H9' mutant, is engineered to have high affinity for the IL-2 receptor beta (CD122) and gamma (CD132) subunits while exhibiting significantly reduced affinity for the alpha subunit (CD25). This selective binding profile is intended to preferentially activate effector CD8+ T cells and natural killer (NK) cells over regulatory T cells (Tregs), thereby enhancing antitumor immunity while minimizing systemic toxicities such as vascular leak syndrome. The fusion to MSA extends the circulatory half-life of the cytokine in murine models, facilitating studies on intratumoral delivery and 'anchoring' strategies that utilize collagen-binding domains to localize the therapeutic effect within the tumor microenvironment.
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