Stat1 (Signal Transducer and Activator of Transcription 1) is a crucial signaling molecule that plays a pivotal role in cells. Upon stimulation by external factors such as cytokines and growth factors, Stat1 is activated through tyrosine kinases (JAK) and mitogen-activated protein kinases (MAPK), leading to the phosphorylation of tyrosine and serine residues at its C-terminus. Phosphorylated Stat1 forms dimers and translocates into the nucleus, binding to specific DNA sequences to activate the transcription of target genes. Stat1 plays a crucial role in the immune system as a key component of the interferon signaling pathway. It regulates cell proliferation, apoptosis, and differentiation, affecting the growth and migration of tumor cells. Phospho-Stat1 (Tyr701) is a phosphorylated form of Stat1. It results from the phosphorylation of Stat1 at the Tyr701 residue. This phosphorylation event is typically induced by cytokines and growth factors through JAK (Janus kinase) or MAPK (Mitogen-Activated Protein Kinase) signaling pathways. In the nucleus, Phospho-Stat1 (Tyr701) dimers bind to specific DNA sequences known as gamma-activated sequence (GAS) elements in the promoters of target genes. Binding to these sequences leads to the transcriptional activation of those genes, thereby influencing cellular responses to cytokines and growth factors.