Mouse Monoclonal NMI Antibody

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     Anti-NMI Antibody at 1:2000 dilution + A431 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-mouse IgG,  (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 35 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Immunofluorescent analysis of 4% paraformaldehyde-fixed, 0.1% Triton X-100 permeabilized HeLa (human cervical epithelial adenocarcinoma cell line) cells labeling NMI with P33459 at 1/25 dilution, followed by Dylight® 488-conjugated goat anti-mouse IgG   secondary antibody at 1/200 dilution (green). Immunofluorescence image showing cytoplasm and nucleus staining on HeLa cell line. Cytoplasmic actin is detected with Dylight® 554 Phalloidin  at 1/100 dilution (red).The nuclear counter stain is DAPI (blue).    

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     Overlay histogram showing K562 cells stained with P33459(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P33459,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Mouse IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(OJ192088) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was mouse IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

N-myc interactor (NMI) is a protein initially identified through its interaction with N-myc, a member of the Myc oncoprotein family. Structurally, NMI contains a coiled-coil domain that facilitates interactions with various transcription factors and signaling molecules, including STAT proteins (signal transducer and activator of transcription). NMI is implicated in regulating diverse cellular processes, such as cell proliferation, differentiation, and immune responses, particularly within the interferon signaling pathway. Its role in cancer biology is context-dependent, acting as both a tumor suppressor and promoter depending on the cellular environment. For instance, NMI suppresses tumor growth in breast and ovarian cancers by enhancing IFN-γ/STAT1 signaling, while in gliomas, it may promote malignancy by stabilizing oncogenic proteins.

NMI antibodies are critical tools for studying these mechanisms. They enable the detection and quantification of NMI expression in tissues or cell lines via techniques like Western blotting, immunohistochemistry, or immunofluorescence. Research using NMI antibodies has revealed its dysregulation in multiple cancers, often correlating with prognosis. For example, reduced NMI levels in triple-negative breast cancer are linked to poor survival, whereas overexpression in colorectal cancer associates with advanced stages. These antibodies also aid in exploring NMI's interplay with signaling pathways, such as its modulation of STAT activity or crosstalk with MYC proteins. Continued development of high-specificity NMI antibodies remains essential for unraveling its complex roles in health and disease.