Recombinant Dog B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active)

CD20 presents a significant challenge as a multi-pass transmembrane target, and this virus-like particle (VLP) format preserves the native conformation of full-length canine CD20 (aa 1–297) by displaying it within a membrane context—critical for generating conformationally relevant immune responses and accurate binding data. Functional ELISA confirms that immobilized dog CD20-VLPs bind an anti-CD20 recombinant antibody with an EC50 of 147.3–199.0 ng/mL, validating the protein's suitability as an antigen for therapeutic antibody screening, cross-reactivity assessment, and immunization campaigns targeting canine lymphoma. The mammalian expression system ensures proper folding and post-translational modifications, while endotoxin levels below 1.0 EU/μg satisfy criteria typical for cell-based functional assays and in vivo immunization studies in veterinary oncology models. The C-terminal 10×His tag, detectable under denaturing conditions, supports use in Western blot-based quality control without interfering with native-conformation binding assays.