Clone REAL627 is an antibody fragment derived from the full CD223 antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAlease Complex to bind markers with high avidity.
Clone REAL627 recognizes the human CD223 antigen, a single-pass type I membrane protein also known as lymphocyte activation gene 3 protein (LAG-3). CD223 is a CD4 homolog with four extracellular Ig superfamily domains. Similar to CD4, CD223 oligomerizes at the surfaces of T cells and binds to MHC II on antigen presenting cells but with significantly higher affinity than CD4. CD223 is expressed on activated CD4
+ and CD8
+ T lymphocytes where it associates with the CD3–TCR complex at the cell surface and negatively regulates signal transduction. As a consequence, it negatively regulates T cell proliferation, function, and homeostasis. There is also increasing evidence of its involvement in regulatory function of tumor-infiltrated T cells in cancer, such as in Hodgkin’s lymphomas and in prostate cancer. CD223 is also expressed on activated natural killer (NK) cells, B cells, and plasmacytoid dendritic cells (pDCs).
The REAlease Kits consist of the respective fluorochrome-conjugated REAlease Complexes and the REAlease Support Kit for removal of the REAlease Complexes and optional relabeling with different fluorochrome-conjugated REAlease Complexes.
