Recombinant MAEA protein (His tag)

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Recombinant Human E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) fragment (amino acids 1-396) is a high-purity protein designed for studying ubiquitination mechanisms and cellular proliferation. This fragment fully encompasses the LisH and CTLH functional domains, making it an ideal tool for domain-specific functional assays and interaction studies.

The full-length MAEA protein serves as a core component of the CTLH E3 ubiquitin-protein ligase complex, which accepts ubiquitin from UBE2H and mediates ubiquitination and proteasomal degradation of the transcription factor HBP1. It is essential for normal cell proliferation and plays a critical role in erythroblast enucleation during erythrocyte maturation, macrophage development, and erythroblastic island formation. MAEA mediates attachment between erythroid cells and macrophages, inhibiting apoptosis and regulating actin distribution via association with F-actin. It localizes to the cytoplasm, nucleus (including nucleoplasm and matrix), cell membrane, and cytoskeleton, with dynamic distribution during cell division phases, suggesting roles in nuclear architecture and cytokinesis.