Human CD27 Protein, ECD (Extracellular Domain), Fc-fusion, Recombinant

Description :
CD27 is a single-pass, type I transmembrane glycoprotein in the TNF receptor superfamily (TNFRSF7). CD27 is expressed as a disulfide­linked homodimer on the cell surface. Proteolytic cleavage of CD27 results in the shedding of a 28­32 kDa fragment of the extracellular domain (ECD) with three TNFR cysteine­rich repeats. The expression of CD27 is limited to cells of the lymphoid lineage. CD27 is weakly expressed on naïve T cells and NK cells and is up­regulated upon cell activation. It is also up­regulated on activated germinal center B cells, plasma cells, and a subset of memory B cells. CD27 acts as a co­stimulatory molecule that supports lymphocyte activation and survival. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by a TNF-like ligand CD70 on lymphocytes and dendritic cells. CD27 binds to the transmembrane glycoprotein CD70 that is expressed on activated B cells, activated T cells, and dendritic cells. CD27 transduces signals and subsequently leads to the activation of NF-κB and JNK pathways that contribute to the activation and survival of T cells and NK cells as well as the long-term maintenance of T cell immunity. CD27 also plays a key role in regulating B-cell differentiation, activation and immunoglobulin synthesis. Ligation of CD27 on B cells promotes germinal center formation and the expansion and affinity maturation of memory B cell responses. Mutations in the CD27 gene are associated with an autosomal recessive immunodeficiency disorder, lymphoproliferative syndrome 2 (LPFS2).