Anti-NMI / N-myc and STAT interactor / N-Myc Interactor, clone PCRP-NMI-1C1

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Nmi (for N-Myc interactor) is an interferon inducible protein that associates with multiple transcription factors, including c-Myc, n-Myc, Max, and c-Fos, which contain bHLH-ZIP, bHLH, or Zip domains. Nmi is ubiquitously expressed at low levels throughout various fetal and adult tissues and at higher levels in myeloid leukemias and cell lines overexpressing c-Myc. In addition to binding Myc proteins, Nmi also associates with the Stat family of transcription factors, where it enhances Stat-dependent transcription. Although Nmi lacks an intrinsic DNA binding or activation domain, Nmi enhances the transcriptional activity of the Stat proteins, in response to cytokine stimulation, by recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. In vitro studies indicate that Nmi, expressed in conjunction with CBP, enhances the transcriptional responsiveness of Stat5 to IL-2 stimulation five-fold over CBP alone by increasing the affinity of Stat proteins for CBP/p300. Protein function: Acts as a signaling pathway regulator involved in innate immune system response (PubMed:9989503, PubMed:26342464, PubMed:29038465, PubMed:29350881). In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude of signals for development and homeostasis (PubMed:9989503, PubMed:29377960). Enhances the recruitment of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased STAT1- and STAT5-dependent transcription (PubMed:9989503). In response to interferon IFN-alpha, associates in a complex with signaling pathway regulator IFI35 to regulate immune response, the complex formation prevents proteasome-mediated degradation of IFI35 (PubMed:10779520, PubMed:10950963). In complex with IFI35, inhibits virus-triggered type I IFN-beta production when ubiquitinated by ubiquitin-protein ligase TRIM21 (PubMed:26342464). In complex with IFI35, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries (PubMed:29350881). Negatively regulates virus-triggered type I interferon/IFN production by inducing proteosome-dependent degradation of IRF7, a transcriptional regulator of type I IFN, thereby interfering with cellular antiviral responses. Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation, when actively released by macrophage to the extracellular space during cell injury or pathogen invasion (PubMed:29038465). Macrophage-secreted NMI activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 binding and activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of proinflammatory cytokines (PubMed:29038465). [The UniProt Consortium]