CD19 (Cluster of differentiation 19), also known as B-lymphocyte antigen CD19, is a 95 kDa transmembrane glycoprotein on the surface of the immunoglobulin superfamily (IgSF) and classified as a type I one-pass transmembrane protein. It maps to the short arm of chromosome 16p11.2 encoded by the 7.41 kilobite CD19 gene that produces a 556-amino acid protein with two extracellular C-type IgSF domains together with a 242-residue cytoplasmic tail that exhibits highly conservation between mouse and human. The CD19 molecules are expressed from the earliest stage of B cells development until plasma cells terminal differentiation. It can associate with the B cell antigen receptor (BCR), CD81 (TAPA-1), CD38, CD21, CD22 and CD225 to establish intrinsic B cell signaling and reduce the thresholds. CD47 molecule, also referred to IAP (Integrin associated protein), OA3 or MER6, is a 35 kDa transmembrane glycoprotein of 323 amino acids and belongs to the immunoglobulin (Ig) superfamily. In humans, this ubiquitously expressed cell surface protein is encoded by the gene mapping at the chromosome 3q13.12. CD47 plays a pivotal role in self-recognition and regulates the innate immunity by acting as an inhibitory signal for phagocytosis through macrophages, neutrophils, and dendritic cells. One critical mechanism under CD47-mediated immune evasion is that it can interact with SIRPα (Signal regulatory protein-alpha) expressed on myeloid cells, ultimately delivering an anti-phagocytic signal. Various solid and hematologic carcinomas exploit CD47 expression so as to escape immunological eradication. And its overexpression is clinically associated with poor prognoses.