PDCD1LG2 Human

PD-L2 was discovered in the early 2000s as part of the B7 family of immune regulatory molecules. It is a type I transmembrane protein with an extracellular domain that interacts with PD-1. The interaction between PD-1 and its ligands, PD-L1 and PD-L2, plays a significant role in maintaining immune homeostasis and preventing autoimmunity by inhibiting T cell activation and proliferation .

PD-L2 is primarily expressed on dendritic cells and macrophages. Its primary function is to modulate the immune response by binding to PD-1 on T cells, leading to the inhibition of T cell receptor signaling. This interaction results in the suppression of T cell activation, cytokine production, and cytotoxic activity, thereby promoting immune tolerance and preventing excessive immune responses .

PD-L2, along with PD-L1, has been implicated in the immune evasion mechanisms of various cancers. Tumor cells can upregulate PD-L2 expression to inhibit anti-tumor immune responses, allowing them to escape immune surveillance. This has led to the development of immune checkpoint inhibitors targeting the PD-1/PD-L1/PD-L2 pathway as a therapeutic strategy in cancer treatment .

Human recombinant PD-L2 is produced using recombinant DNA technology, where the PDCD1LG2 gene is cloned into an expression vector and introduced into host cells, such as bacteria or mammalian cells. These host cells then produce the PD-L2 protein, which can be purified and used for research or therapeutic purposes. Recombinant PD-L2 is used in various studies to understand its role in immune regulation and to develop novel immunotherapies .

The blockade of the PD-1/PD-L2 interaction has shown promising results in clinical trials for various cancers. By inhibiting this pathway, immune checkpoint inhibitors can enhance the anti-tumor activity of T cells, leading to improved clinical outcomes in patients with cancers such as melanoma, lung cancer, and renal cell carcinoma .