Description | The PC61.5 antibody is specific for mouse CD25, a 55 kDa surface protein also known as the Interleukin-2 Receptor alpha chain, or IL- 2R alpha. CD25 may bind IL-2 by itself, although with low affinity and without induction of cell signaling. CD25 is also expressed within a high-affinity complex, along with the IL-2R beta chain (CD122) and the common gamma chain (CD132), to form a signaling receptor complex. Expression of CD25 varies during developmental stages of T and B cells, is induced on activated mature T and B cells, and is present on subsets of dendritic cells. CD25 signaling as part of the IL-2 receptor complex triggers T cell activation and proliferation, as well as modulating the differentiation and function of Th17 cells, T regulatory (Treg) cells, and dendritic cells. The PC61.5 antibody is used as a marker for T cells, B cells and dendritic cell subsets. Expression of CD25, CD4 and the transcription factor Foxp3 is regarded as a phenotypic signature for Treg cells. As such, this antibody is widely used for depletion of Treg cells in vivo, as well as to distinguish Treg cells from naive or conventional T cells which are CD25-. Target Information: The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolyisis. Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is presently unknown. Mutations in this gene are associated with interleukin 2 receptor alpha deficiency.[provided by RefSeq, Nov 2009]. |