Recombinant ILF2 protein (His tag)

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Recombinant Human Interleukin enhancer-binding factor 2 (ILF2) fragment (amino acids 1-390) is a high-purity protein designed for studying chromatin interactions, transcriptional regulation, and RNA-binding functions. This fragment fully encompasses the DZF domain, making it an ideal tool for investigating specific domain-mediated activities in immune response, viral inhibition, and cell cycle progression.

Interleukin enhancer-binding factor 2 (ILF2), also known as Nuclear factor of activated T-cells 45 kDa, is a chromatin-interacting protein that forms a stable heterodimer with ILF3. It plays critical roles in transcription, innate immunity, and cell growth by regulating mitotic gene expression and competing with STAU1/STAU2-mediated mRNA decay. ILF2 is essential for the nuclear reshuttling of ILF3 and supports mitotic progression and cytokinesis. Additionally, it inhibits various viruses, including Japanese encephalitis virus and enterovirus 71, and positively influences HIV-1 production by stabilizing viral RNA in complex with ILF3. The protein localizes to the nucleus, nucleolus, and cytoplasm, and is found in cytoplasmic mRNP granules containing untranslated mRNAs, highlighting its involvement in mRNA metabolism and cellular defense mechanisms.