There are three families of IFNs: types I, II, and III. In humans, type I contains IFN-α (13 different subtypes), IFN-β (also known as IFN-β1), IFN-ε, IFN-κ, and IFN-ω.

The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins. Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB.

Heterochromatin protein 1 (HP1) is a family of heterochromatic adaptor molecules involved in both gene silencing and higher-order chromatin structure (1).

With the rapid development of tumor immunotherapy, precise assessment of the tumor microenvironment (TME) has become a core prerequisite for interpreting immune escape mechanisms, screening populations benefiting from immunotherapy, and optimizing treatment regimens. Traditional single-marker immunohistochemistry (IHC) and immunofluorescence (IF) techniques can only detect a single marker, failing to comprehensively present the complex composition of immune cell subsets, marker co-expression characteristics, and intercellular spatial relationships in the TME, which is insufficient to meet the needs of precise immunotherapy research and clinical applications. Against this backdrop, multiplex immunohistochemistry (mIHC) and multiplex immunofluorescence (mIF) technologies have emerged and rapidly iterated, becoming core technologies for parsing TME heterogeneity and mining immunotherapy biomarkers due to their advantage of simultaneously detecting multiple markers in tissue sections.

Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin.

The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation.

DNA double-strand breaks (DSBs) are potentially hazardous lesions that can be induced by ionizing radiation (IR), radiomimetic chemicals, or DNA replication inhibitors.

Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2).