Activation-Induced Tumor Necrosis Factor Receptor Ligand (AITRL), also known as Tumor Necrosis Factor Superfamily Member 18 (TNFSF18), is a crucial protein involved in immune modulation. AITRL is a member of the tumor necrosis factor superfamily and plays a significant role in regulating immune responses. The recombinant form of AITRL, produced in Escherichia coli, is widely used in research to study its biological functions and therapeutic potential.
AITRL is a transmembrane protein that consists of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain, and a 128 amino acid extracellular domain . The recombinant human AITRL is typically produced in Escherichia coli as a single, non-glycosylated polypeptide chain containing 129 amino acids (72-199) with a molecular mass of approximately 14.6 kDa . The protein is purified using proprietary chromatographic techniques to achieve high purity levels, often greater than 90% as determined by SDS-PAGE .
AITRL is primarily expressed in endothelial cells and interacts with its receptor, Activation-Induced Tumor Necrosis Factor Receptor (AITR), also known as TNFRSF18 . This interaction leads to downstream signaling events that modulate immune cell function. AITRL plays a pivotal role in T-cell activation, proliferation, and differentiation. It can stimulate effector T-cell responses while also promoting the development and function of regulatory T cells, thus maintaining immune homeostasis .
The dysregulation of AITRL signaling has been implicated in various immune-related disorders, including autoimmune diseases, allergic reactions, and cancer . Due to its significant role in immune regulation, AITRL has emerged as a potential target for therapeutic interventions. Researchers are exploring the use of recombinant AITRL in developing treatments for these conditions, aiming to modulate immune responses effectively.