Recombinant Human MHC class I chain-related molecule B (MICB), partial (Active)

MICB functions as a stress-induced ligand for the activating receptor NKG2D on natural killer cells and CD8+ T cells, making it a critical target in cancer immunology and transplant rejection research. This partial construct spanning residues 204–297 captures the α3 domain, and mammalian expression ensures native glycosylation patterns that preserve conformational epitopes essential for antibody recognition. Functional ELISA validation demonstrates specific binding to an anti-MICA/B recombinant antibody with an EC50 of 26.77–32.93 ng/mL, providing quantitative evidence that this protein supports therapeutic antibody epitope mapping, competitive inhibition screening, and blocking antibody validation studies. The combination of >95% purity by SDS-PAGE and <1.0 EU/μg endotoxin meets the quality thresholds commonly required for ligand-binding assays, surface plasmon resonance affinity characterization, and biolayer interferometry experiments where low background interference is critical for accurate kinetic measurements.