This product is an unconjugated, non-therapeutic recombinant analog of the anti-CD47 antibody lemzoparlimab, supplied strictly for research use only. It is built as a human IgG1 directed against human CD47 and reproduces the target specificity of the originator molecule so that laboratories can use it as a reference or tool reagent, not as the clinical drug. It is not intended for human or veterinary use. Typical research applications include CD47 binding and blockade assays, characterization of the CD47-SIRPalpha "don't eat me" axis, macrophage phagocytosis and ADCC-format assays, flow cytometry, and use as an isotype-matched positive control or benchmarking comparator when developing new CD47-targeted biologics. The reagent is available at low endotoxin grade (research grade less than 1 EU/mg, ultra-low less than 0.5 EU/mg) and in bulk milligram-to-gram quantities to support screening, assay standardization, and preclinical workflows. Because it is a research-grade analog rather than a clinical product, it is appropriate for in-vitro mechanistic studies, controls, and biosimilar/comparator development rather than any therapeutic application.
CD47 (integrin-associated protein; UniProt Q08722) is a broadly expressed five-pass transmembrane glycoprotein of the immunoglobulin superfamily. Its principal counter-receptor is SIRPalpha (signal regulatory protein alpha) on macrophages and other myeloid cells. Engagement of macrophage SIRPalpha by CD47 delivers an inhibitory "don't eat me" signal that suppresses phagocytosis, allowing healthy cells to avoid clearance. Many tumors overexpress CD47 to evade macrophage-mediated destruction, which is why the CD47-SIRPalpha axis is an intensively studied immuno-oncology checkpoint. CD47 also interacts with thrombospondin-1 and with integrins, contributing to cell adhesion, migration, and signaling. Blocking CD47 or the CD47-SIRPalpha interaction can restore pro-phagocytic signaling; a key liability of CD47 targeting is on-target binding to CD47 on erythrocytes, which motivates engineering approaches aimed at reducing red-blood-cell binding.