Recombinant Human ULBP2 protein (His tag C-Terminus)

補足情報

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ULBP2 also known as UL16-binding protein 2 and N2DL2 is a glycoprotein with a mass of approximately 30 kDa. It belongs to the family of NKG2D ligands and plays an essential role in the immune response. This protein is expressed on the surface of a variety of cells including epithelial cells fibroblasts and activated immune cells. Its expression can be induced by cellular stress infection or transformation making it an important player in the regulation of the immune system.

Biological function summary

The function of ULBP2 is to facilitate the activation of natural killer (NK) cells and cytotoxic T lymphocytes through binding to the NKG2D receptor. ULBP2 is not a part of a complex but acts independently to trigger immune responses. By interacting with NKG2D ULBP2 promotes the release of cytokines and enhances the cytolytic activity of these immune cells leading to the destruction of infected or transformed cells. This mechanism allows the immune system to efficiently target and eliminate compromised cells.

Pathways

The interaction between ULBP2 and the NKG2D receptor forms a critical part of the immune surveillance pathway. This pathway detects and responds to cellular abnormalities such as tumorigenesis or viral infections. ULBP2's activity relates closely with other NKG2D ligands and components of the immune checkpoint pathways notably involving proteins like MICA and MICB. Additionally ULBP2’s interaction impacts the balance between activating and inhibitory signals within the NK cell cascade thereby influencing immune system homeostasis.

ULBP2 expression has significant implications in cancer and autoimmune conditions. Elevated levels of ULBP2 are frequently associated with various types of cancer where they can either stimulate anti-tumor immunity or be shed to evade immune detection. In this context the protein interacts with NKG2D which is also expressed on tumor-infiltrating lymphocytes. Additionally altered expression of ULBP2 has been observed in inflammatory disorders potentially contributing to tissue damage due to sustained immune activation. Understanding these interactions is important for developing therapeutic strategies targeting ULBP2-related pathways.