1. Recombinant Proteins
  2. Immune Checkpoint Proteins
  3. Inhibitory checkpoint molecules
  4. CD47 & SIRPα

CD47 (also known as IAP, MER6, or OA3), a transmembrane protein, belongs to the immunoglobulin superfamily (IgSF) that consists of a single extracellular V-set IgSF domain, a presenilin domain with 5 membrane-spanning sections and a short cytoplasmic domain with ITIM motifs. CD47 is highly expressed in most cell types and often overexpressed on cancer cells. Important cellular ligands for CD47 are the signal regulatory proteins (SIRPs) SIRPα and SIRPγ. SIRPα is also a transmembrane protein that contains three Ig-like domains in its extracellular region and two tyrosine phosphorylation sites in its C-terminal cytoplasmic region. SIRPα is expressed on all myeloid cell types, including monocytes, macrophages, neutrophils, a subset of dendritic cells, and microglia. Overexpression of CD47 is through to be a key mechanism of tumor cell immune escape. Widely regarded as a “don't eat me” signal, CD47 helps maintain immunotolerance by non-malignant cells under physiological conditions, but can also aid in the survival of cancer cells in various cancer types. In many cancer types, CD47 binding to SIRPα triggers an inhibitory signaling pathway that leads to the evasion of malignant cells from phagocytosis by macrophages. Blocking CD47-SIRPα interactions has been shown to promote the destruction of cancer cells by phagocytes, including mac rophages and neutrophils. Furthermore, there is growing evidence that targeting of the CD47-SIRPα axis may also promote antigen-presenting cell function and thereby stimulate adaptive T cell-mediated anti-cancer immunity.

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