CD27 is a Type I transmembrane protein. It is constitutively expressed on the majority of T cells, memory B cells, plasma cells, and natural killer (NK) cells . The extracellular domain of CD27 is responsible for binding to CD70, which is primarily expressed on antigen-presenting cells (APCs) . The interaction between CD27 and CD70 promotes T cell activation and maturation, working in concert with T cell receptor engagement .
The CD27/CD70 axis is considered a costimulatory immune checkpoint. This interaction is essential for the survival and antitumor activity of T cells . CD27 signaling enhances the survival of activated T cells and contributes to the formation of memory T cells. It also plays a role in the differentiation and function of B cells, particularly in the production of immunoglobulins .
Recombinant human CD27 is often produced as a fusion protein. For example, a soluble form of human CD27 can be generated by fusing the N-terminal extracellular domain of CD27 to the Fc domain of human IgG1. This recombinant protein is produced in CHO cells and purified by affinity chromatography . The recombinant CD27-Fc fusion protein has an apparent molecular weight of approximately 55 kDa on an SDS-PAGE gel .
Recombinant CD27 has several applications in research and therapeutic development: