Recombinant MGN protein (His tag)

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Recombinant Protein mago nashi homolog (MAGOH) fragment (residues 1-146) is a high-purity, stable, and soluble protein designed for structural and biochemical studies. This fragment captures a key functional domain of MAGOH, a core component of the exon junction complex (EJC) and spliceosome, enabling research into pre-mRNA splicing, nonsense-mediated decay, and mRNA metabolism.

Protein mago nashi homolog (MAGOH) is a human protein essential for pre-mRNA splicing as part of the spliceosome and functions redundantly with MAGOHB as a core component of the exon junction complex (EJC). The EJC marks exon-exon junctions in mature mRNAs and influences downstream processes including nuclear mRNA export, subcellular localization, translation efficiency, and nonsense-mediated decay (NMD). MAGOH, in a heterodimer with RBM8A, inhibits the ATPase activity of EIF4A3 to stabilize the EJC on spliced mRNAs and interacts with PYM1 to facilitate EJC disassembly and enhance translation. It also modulates splicing of apoptotic genes like BCL2L1/Bcl-X, inhibiting proapoptotic isoforms. MAGOH localizes to the nucleus, nuclear speckles, and cytoplasm, traveling with the EJC-bound mRNA, and is detected in granule-like structures in the dendroplasm, highlighting its role in dynamic mRNA metabolism.