The Interleukin-2 receptor (IL-2R), also known as CD25, is a critical component of the immune system. It plays a pivotal role in the regulation of immune responses by mediating the effects of interleukin-2 (IL-2), a cytokine that promotes the growth, differentiation, and survival of T cells. The IL-2 receptor is composed of three subunits: alpha (IL-2Rα or CD25), beta (IL-2Rβ), and the common gamma chain (IL-2Rγ). The high-affinity IL-2 receptor is formed by the assembly of these three subunits .
CD25, the alpha chain of the IL-2 receptor, is a 55 kDa protein that binds IL-2 with low affinity on its own. However, when combined with the beta and gamma chains, it forms a high-affinity receptor complex. This receptor complex is essential for the IL-2-mediated signaling pathways that regulate T cell proliferation and differentiation .
CD25 is constitutively expressed at high levels on regulatory T cells (Tregs) and transiently on activated effector T cells (Teff). The expression of CD25 is a hallmark of Treg cells, which play a crucial role in maintaining immune tolerance and preventing autoimmune diseases .
The rat anti-mouse CD25 antibody is a monoclonal antibody that specifically targets the CD25 molecule on mouse cells. This antibody is commonly used in immunological research to study the expression and function of CD25 in various mouse models. It is particularly useful in flow cytometry, immunohistochemistry, and other immunoassays to identify and isolate CD25-expressing cells .
One of the widely used clones of rat anti-mouse CD25 antibody is PC61. This clone has been extensively characterized and is known for its high specificity and affinity for mouse CD25. The PC61 antibody can be conjugated to various fluorochromes or enzymes to facilitate its detection in different experimental setups .
The rat anti-mouse CD25 antibody has several important applications in immunological research: