History of Interleukin 2

History of Interleukin 2

IL-2 (il 2 antibody) is historically significant since it was the first type I cytokine to be cloned, as well as the first type I cytokine to have a receptor component cloned and the first short-chain type I cytokine to have its receptor structure solved. Many general concepts have emerged from research on this cytokine, including the fact that it was the first cytokine to be shown to function in a growth factor-like manner via specialized high-affinity receptors, similar to the growth factors researched by endocrinologists and biochemists. IL-2, whether recombinant or purified, had been tested in dozens of clinical trials, either alone or in conjunction with other medications, or via cell treatments, in which cells were removed from patients, stimulated with IL-2, and then reinfused.

IL 2 Receptor

IL-2 binds to the IL-2 receptor, which comes in three forms and is made up of three different proteins called "chains": (alpha) (also known as IL-2R, CD25, or Tac antigen), (beta) (also known as IL-2R, or CD122), and (gamma) (also known as IL-2R, c, common gamma chain, or CD132); these subunits are also found in other cytokines [1]: 713 The type I cytokine receptor family includes the and chains of the IL-2R.