UBE2B, also known as RAD6B or E2-17kDa, is a member of the ubiquitin-conjugating enzyme family. It facilitates the transfer of ubiquitin to target proteins, marking them for proteasomal degradation or functional modulation . The UBE2B antibody is a monoclonal reagent (clone 1F11) developed for applications such as Western blotting, ELISA, and immune cell studies . Its specificity for human UBE2B makes it valuable for investigating the enzyme’s role in diseases, particularly cancer .
UBE2B has emerged as a prognostic biomarker and therapeutic target in cancers, notably esophageal carcinoma (ESCA). Key findings include:
Pathway Involvement: UBE2B activates oncogenic pathways such as TNF-α/NF-κB signaling, epithelial-mesenchymal transition (EMT), and hypoxia response .
Immune Modulation: UBE2B expression is linked to altered immune infiltration, including increased CD8+ T cells and macrophages, and reduced Th17 cells in ESCA tumors .
Knockdown Studies: Silencing UBE2B in ESCA cell lines suppresses proliferation and migration, confirming its oncogenic role .
Immune Correlation: UBE2B expression positively correlates with B cell activation and receptor signaling pathways (GO:0050853, p = 0.002) .
UBE2B’s involvement across multiple cancer types highlights its potential as a pan-cancer target. Current research aims to: