This product is an unconjugated, non-therapeutic recombinant analog of epratuzumab, a humanized IgG1 kappa monoclonal antibody directed against human CD22 (Siglec-2). It is supplied for research use only and is not the clinical drug, nor is it intended for human or veterinary use. Built around the CD22 target, the analog reproduces the antigen-binding specificity of the originator, making it a convenient, well-defined reagent for laboratory investigation of CD22 biology and of anti-CD22 antibody behavior. Typical research applications include use as a binding and specificity control, a benchmark or reference antibody in assay development, a positive control in B-cell characterization, and a building block for antibody-drug conjugate (ADC) and effector-function studies. It is produced at research grade with low endotoxin (<1 EU/mg; ultra-low <0.5 EU/mg options), and is available in bulk milligram-to-gram quantities and in-vivo-standard preparations. The consistent, characterized format supports reproducible comparisons across experiments and lots without the constraints or cost of sourcing clinical material.
CD22 (Siglec-2; UniProt P20273) is a type I transmembrane sialic-acid-binding immunoglobulin-like lectin expressed almost exclusively on B lymphocytes. It appears on the surface during B-cell maturation, is present on mature IgM+/IgD+ B cells, and is generally lost upon differentiation to plasma cells. Its extracellular region contains seven immunoglobulin-like domains; the membrane-distal domain recognizes alpha-2,6-linked sialic acids, mediating homotypic and heterotypic cell interactions. The cytoplasmic tail carries immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that, upon phosphorylation, recruit the phosphatase SHP-1 to dampen B-cell receptor signaling, positioning CD22 as a key inhibitory co-receptor that sets B-cell activation thresholds and supports peripheral tolerance. CD22 also undergoes rapid internalization on antibody engagement. Its restricted B-lineage expression and efficient endocytosis make it an attractive target for antibody-based and conjugate approaches in B-cell malignancies and autoimmunity.