STING1 (Stimulator of Interferon Response cGAMP Interactor 1, also known as TMEM173) is a critical endoplasmic reticulum-resident adaptor protein that serves as a central node in the innate immune system's response to cytosolic DNA ^[1]. Expressed across various tissues, with notable enrichment in immune cells such as dendritic cells, macrophages, and lymphocytes, STING detects cyclic dinucleotides produced by the enzyme cGAS upon sensing foreign or aberrant self-DNA in the cytoplasm ^[2]. This recognition triggers a conformational change in STING, facilitating its translocation and subsequent recruitment and activation of the kinase TBK1, which in turn phosphorylates transcription factors like IRF3 and NF-κB. Activation of these pathways precipitates the rapid production of type I interferons and pro-inflammatory cytokines, orchestrating essential host defense mechanisms against intracellular pathogens, particularly viruses and bacteria ^[2-3]. Beyond infectious diseases, dysregulation of STING signaling is increasingly recognized in the pathogenesis of autoinflammatory conditions, such as severe gain-of-function mutations causing STING-associated vasculopathy with onset in infancy (SAVI), and contributes complexly to the tumor microenvironment, influencing both anti-tumor immunity and inflammation ^[3-4]. The pivotal role of STING in sensing danger signals and initiating inflammatory cascades positions it as a significant target for therapeutic intervention in a range of immune-mediated diseases and cancers. The huSTING1 mouse is a humanized model constructed by replacing the sequence of the mouse Sting1 gene in situ with the corresponding sequence from the human STING1 gene. The huSTING1 mice can be used to study the pathogenesis of immune-mediated diseases and cancers, as well as for STING1-targeted drug development.