Adgrl2-3xGGGGS-mCherry Mouse

The ADGRL2 gene (Adhesion G Protein-Coupled Receptor L2), also known as latrophilin 2, encodes a member of the adhesion G protein-coupled receptor (aGPCR) family, which are characterized by a long N-terminal domain involved in cell-cell and cell-matrix interactions ^[1]. The encoded protein, ADGRL2, is involved in various physiological processes, including cell adhesion, neuronal development, regulation of exocytosis (e.g., as a low-affinity receptor for alpha-latrotoxin), and maintaining intestinal homeostasis ^[2]. It is expressed in numerous tissues, with notable expression in the central nervous system (neurons, hippocampus), intestinal epithelium, and specifically, its expression is strongly upregulated during keratinocyte differentiation in epidermal tissue ^[3]. Dysregulation or variations in ADGRL2 have been associated with a range of conditions, including neurodegenerative diseases (like Alzheimer's and Parkinson's), inflammatory bowel diseases (Crohn's disease, ulcerative colitis), certain autoimmune diseases (rheumatoid arthritis, systemic lupus erythematosus, multiple sclerosis), and even metabolic syndrome and cocaine use disorder.

Adgrl2-3xGGGGS-mCherry mice are constructed by replacing the partial exon 1 coding region of the mouse Adgrl2 gene with HA signal peptide - HA tag - Mouse Adgrl2 CDS (without signal peptide) - 3xGGGGS - mCherry - rBG pA cassette using gene editing technology. The Adgrl2-3xGGGGS-mCherry mouse carries a red fluorescent protein (mCherry) expression cassette, making it a precise research model that maintains protein function while offering fluorescence visualization. This model is valuable for several key areas of study. For instance, it can be used for the spatio-temporal dynamic analysis of the Adgrl2 gene expression profile. Researchers can also utilize it for investigating neuronal development and synapse formation mechanisms. Furthermore, it enables live-animal dynamic tracking and real-time imaging observation, providing invaluable insights. Lastly, this model is well-suited for systematic studies of protein interaction networks and downstream signaling pathways.