Recombinant Human MIB2 protein

MIB2 (Mind Bomb 2) is an E3 ubiquitin ligase that plays a critical role in regulating ubiquitination-dependent signaling pathways, particularly the Notch signaling cascade. As a member of the MIB protein family, it facilitates the transfer of ubiquitin molecules to specific substrate proteins, marking them for proteasomal degradation or functional modulation. MIB2 is structurally characterized by multiple functional domains, including a MIB-specific N-terminal domain, tandem zinc-finger motifs, and a C-terminal RING finger domain essential for its E3 ligase activity. These domains enable MIB2 to interact with substrates like the Notch receptor ligands (e.g., Delta, Jagged) and mediate their ubiquitination, thereby influencing cell-cell communication, cell fate determination, and developmental processes.

Recombinant MIB2 proteins are engineered using expression systems (e.g., bacterial, insect, or mammalian cells) to produce purified, functional MIB2 for experimental studies. These proteins retain key biochemical properties, allowing researchers to investigate MIB2’s enzymatic mechanisms, substrate specificity, and regulatory roles in vitro or in cellular models. MIB2’s involvement in critical pathways has linked it to diseases, including cancers and neurological disorders, where dysregulated ubiquitination contributes to pathogenesis. For instance, aberrant MIB2 expression may disrupt Notch signaling, affecting tissue homeostasis. Recombinant MIB2 thus serves as a tool for drug discovery, enabling high-throughput screening for inhibitors or activators to restore pathway balance. Its study also sheds light on the broader ubiquitin-proteasome system, advancing therapeutic strategies targeting E3 ligases.