22RV1-PDL1-GFP-Luc2-Cell-Line

PDL1 encoded by this gene is an immune inhibitory receptor ligand that is expressed by hematopoietic and non-hematopoietic cells, such as T cells and B cells and various types of tumor cells. The encoded protein is a type I transmembrane protein that has immunoglobulin V-like and C-like domains. Interaction of this ligand with its receptor inhibits T-cell activation and cytokine production. During infection or inflammation of normal tissue, this interaction is important for preventing autoimmunity by maintaining homeostasis of the immune response. In tumor microenvironments, this interaction provides an immune escape for tumor cells through cytotoxic T-cell inactivation. Mice deficient for this gene display a variety of phenotypes including decreased allogeneic fetal survival rates and severe experimental autoimmune encephalomyelitis.
Luciferase is an oxidative enzyme that can produce bioluminescence with addition of luciferin, but doesn’t need an external light source unlike fluorescent proteins. Photo emission can be detected directly by light sensitive devices. Such as luminometers or modified microscopes. Luciferase is widely used in many fields of biological research, such as transcriptional activity, kinase or other enzyme activity, cellular ATP level, and whole animal imaging.
Green fluorescent protein (GFP) is a β - barrel protein 1 composed of 238 amino acids with a molecular weight of approximately 27 kDa. GFP was isolated from the crystal jellyfish Aequorea Victoria. GFP can convert the blue fluorescence emitted by jellyfish luminescent protein through chemical reactions into green fluorescence through energy transfer. The excitation wavelength of GFP is 488 nm, and there is an emission peak at approximately 507 nm.