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human nelfc  (Addgene inc)


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    Addgene inc human nelfc
    Figure 4. <t>NELFC</t> binding-deficient mutants of NELFB are retained in the cytoplasm. A, Super-resolution 3D structured illumination microscopy-based immunofluorescence image of NELFB (blue) and DAPI (yellow) in WT cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. B, immunofluorescent staining of NELFB and DAPI in WT, MT183, MT194, and MT486 cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. C, Western blotting of different NELF subunits in ectopic WT and MT194 clones. Tubulin and H3 are used as markers for cytosol and nuclear fractions, respectively. Two independent clones for each cell line were used and the experiments were done with two independent repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE in MT194 cell clones. D, Western blotting of NELF subunits <t>in</t> <t>NELFC-AID</t> cells, following treatment of PBS or 0.5 mM IAA for 6 h. GAPDH, ATP5B, and LAMIN B1 were used as markers for cytosol, membrane, and nuclear fractions, respectively. Representative result is shown from three independent biological repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE, despite the reduction of cytoplasmic NELFC. AID, auxin-induced protein degradation; DAPI, 40,6-diamidino-2-phenylindole; IAA, indole-3-acetic acid; NELF, negative elongation factor.
    Human Nelfc, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human nelfc/product/Addgene inc
    Average 93 stars, based on 12 article reviews
    human nelfc - by Bioz Stars, 2026-04
    93/100 stars

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    1) Product Images from "An essential signaling function of cytoplasmic NELFB is independent of RNA polymerase II pausing."

    Article Title: An essential signaling function of cytoplasmic NELFB is independent of RNA polymerase II pausing.

    Journal: The Journal of biological chemistry

    doi: 10.1016/j.jbc.2023.105259

    Figure 4. NELFC binding-deficient mutants of NELFB are retained in the cytoplasm. A, Super-resolution 3D structured illumination microscopy-based immunofluorescence image of NELFB (blue) and DAPI (yellow) in WT cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. B, immunofluorescent staining of NELFB and DAPI in WT, MT183, MT194, and MT486 cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. C, Western blotting of different NELF subunits in ectopic WT and MT194 clones. Tubulin and H3 are used as markers for cytosol and nuclear fractions, respectively. Two independent clones for each cell line were used and the experiments were done with two independent repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE in MT194 cell clones. D, Western blotting of NELF subunits in NELFC-AID cells, following treatment of PBS or 0.5 mM IAA for 6 h. GAPDH, ATP5B, and LAMIN B1 were used as markers for cytosol, membrane, and nuclear fractions, respectively. Representative result is shown from three independent biological repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE, despite the reduction of cytoplasmic NELFC. AID, auxin-induced protein degradation; DAPI, 40,6-diamidino-2-phenylindole; IAA, indole-3-acetic acid; NELF, negative elongation factor.
    Figure Legend Snippet: Figure 4. NELFC binding-deficient mutants of NELFB are retained in the cytoplasm. A, Super-resolution 3D structured illumination microscopy-based immunofluorescence image of NELFB (blue) and DAPI (yellow) in WT cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. B, immunofluorescent staining of NELFB and DAPI in WT, MT183, MT194, and MT486 cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. C, Western blotting of different NELF subunits in ectopic WT and MT194 clones. Tubulin and H3 are used as markers for cytosol and nuclear fractions, respectively. Two independent clones for each cell line were used and the experiments were done with two independent repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE in MT194 cell clones. D, Western blotting of NELF subunits in NELFC-AID cells, following treatment of PBS or 0.5 mM IAA for 6 h. GAPDH, ATP5B, and LAMIN B1 were used as markers for cytosol, membrane, and nuclear fractions, respectively. Representative result is shown from three independent biological repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE, despite the reduction of cytoplasmic NELFC. AID, auxin-induced protein degradation; DAPI, 40,6-diamidino-2-phenylindole; IAA, indole-3-acetic acid; NELF, negative elongation factor.

    Techniques Used: Binding Assay, Microscopy, Staining, Western Blot, Clone Assay, Membrane

    Figure 6. NELFB supports progrowth signaling transduction. A, Western blotting of cell lysates from MEFs depleted of NELFB by Cre-loxP. Representative results from three independent repeats. Asterisks indicate the reduced intensity of phosphorylated proteins. B–D, quantification of phosphorylation of various signaling molecules, which was normalized with total proteins from three independent experiments. Statistics was conducted using multiple t test. E, NELFB-AID and NELFC-AID MEFs were treated with PBS or 0.5 mM IAA and then harvested at different time points. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein and indicated below the corresponding protein. Representative images were shown from three independent repeats. F and G, violin plot distributions of Pol II ChIP-seq reads at the TSS (−0.5 to +0.5kb) and GB (+0.5 to +2.5 kb) in NELFB- AID cells (F) and NELFC-AID cells (G) following treatment of PBS or 0.5 mM IAA for 6 h. Pol II ChIP-seq was from two independent experiments. H, NELFB-AID in MDA-MB-231 cells following IAA treatment. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein Three independent clones were used for the experiment. I, NELFB-AID cell lines that stably expressed EV, WT, or MT194 were treated with IAA. Cell
    Figure Legend Snippet: Figure 6. NELFB supports progrowth signaling transduction. A, Western blotting of cell lysates from MEFs depleted of NELFB by Cre-loxP. Representative results from three independent repeats. Asterisks indicate the reduced intensity of phosphorylated proteins. B–D, quantification of phosphorylation of various signaling molecules, which was normalized with total proteins from three independent experiments. Statistics was conducted using multiple t test. E, NELFB-AID and NELFC-AID MEFs were treated with PBS or 0.5 mM IAA and then harvested at different time points. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein and indicated below the corresponding protein. Representative images were shown from three independent repeats. F and G, violin plot distributions of Pol II ChIP-seq reads at the TSS (−0.5 to +0.5kb) and GB (+0.5 to +2.5 kb) in NELFB- AID cells (F) and NELFC-AID cells (G) following treatment of PBS or 0.5 mM IAA for 6 h. Pol II ChIP-seq was from two independent experiments. H, NELFB-AID in MDA-MB-231 cells following IAA treatment. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein Three independent clones were used for the experiment. I, NELFB-AID cell lines that stably expressed EV, WT, or MT194 were treated with IAA. Cell

    Techniques Used: Transduction, Western Blot, Phospho-proteomics, ChIP-sequencing, Clone Assay, Stable Transfection



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    human nelfc  (Addgene inc)
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    Addgene inc human nelfc
    Figure 4. <t>NELFC</t> binding-deficient mutants of NELFB are retained in the cytoplasm. A, Super-resolution 3D structured illumination microscopy-based immunofluorescence image of NELFB (blue) and DAPI (yellow) in WT cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. B, immunofluorescent staining of NELFB and DAPI in WT, MT183, MT194, and MT486 cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. C, Western blotting of different NELF subunits in ectopic WT and MT194 clones. Tubulin and H3 are used as markers for cytosol and nuclear fractions, respectively. Two independent clones for each cell line were used and the experiments were done with two independent repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE in MT194 cell clones. D, Western blotting of NELF subunits <t>in</t> <t>NELFC-AID</t> cells, following treatment of PBS or 0.5 mM IAA for 6 h. GAPDH, ATP5B, and LAMIN B1 were used as markers for cytosol, membrane, and nuclear fractions, respectively. Representative result is shown from three independent biological repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE, despite the reduction of cytoplasmic NELFC. AID, auxin-induced protein degradation; DAPI, 40,6-diamidino-2-phenylindole; IAA, indole-3-acetic acid; NELF, negative elongation factor.
    Human Nelfc, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human nelfc/product/Addgene inc
    Average 93 stars, based on 1 article reviews
    human nelfc - by Bioz Stars, 2026-04
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Figure 4. NELFC binding-deficient mutants of NELFB are retained in the cytoplasm. A, Super-resolution 3D structured illumination microscopy-based immunofluorescence image of NELFB (blue) and DAPI (yellow) in WT cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. B, immunofluorescent staining of NELFB and DAPI in WT, MT183, MT194, and MT486 cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. C, Western blotting of different NELF subunits in ectopic WT and MT194 clones. Tubulin and H3 are used as markers for cytosol and nuclear fractions, respectively. Two independent clones for each cell line were used and the experiments were done with two independent repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE in MT194 cell clones. D, Western blotting of NELF subunits in NELFC-AID cells, following treatment of PBS or 0.5 mM IAA for 6 h. GAPDH, ATP5B, and LAMIN B1 were used as markers for cytosol, membrane, and nuclear fractions, respectively. Representative result is shown from three independent biological repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE, despite the reduction of cytoplasmic NELFC. AID, auxin-induced protein degradation; DAPI, 40,6-diamidino-2-phenylindole; IAA, indole-3-acetic acid; NELF, negative elongation factor.

    Journal: The Journal of biological chemistry

    Article Title: An essential signaling function of cytoplasmic NELFB is independent of RNA polymerase II pausing.

    doi: 10.1016/j.jbc.2023.105259

    Figure Lengend Snippet: Figure 4. NELFC binding-deficient mutants of NELFB are retained in the cytoplasm. A, Super-resolution 3D structured illumination microscopy-based immunofluorescence image of NELFB (blue) and DAPI (yellow) in WT cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. B, immunofluorescent staining of NELFB and DAPI in WT, MT183, MT194, and MT486 cells. Representative images from three independent repeats were shown. The scale bar represents 20 μm. C, Western blotting of different NELF subunits in ectopic WT and MT194 clones. Tubulin and H3 are used as markers for cytosol and nuclear fractions, respectively. Two independent clones for each cell line were used and the experiments were done with two independent repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE in MT194 cell clones. D, Western blotting of NELF subunits in NELFC-AID cells, following treatment of PBS or 0.5 mM IAA for 6 h. GAPDH, ATP5B, and LAMIN B1 were used as markers for cytosol, membrane, and nuclear fractions, respectively. Representative result is shown from three independent biological repeats. Asterisks indicate elevated levels of cytoplasmic NELFB and NELFE, despite the reduction of cytoplasmic NELFC. AID, auxin-induced protein degradation; DAPI, 40,6-diamidino-2-phenylindole; IAA, indole-3-acetic acid; NELF, negative elongation factor.

    Article Snippet: C-terminal mini-AID– tagged mouse NELFB and human NELFC were cloned into pLenti-6.3/V5-DEST-GFP (Addgene: 40125).

    Techniques: Binding Assay, Microscopy, Staining, Western Blot, Clone Assay, Membrane

    Figure 6. NELFB supports progrowth signaling transduction. A, Western blotting of cell lysates from MEFs depleted of NELFB by Cre-loxP. Representative results from three independent repeats. Asterisks indicate the reduced intensity of phosphorylated proteins. B–D, quantification of phosphorylation of various signaling molecules, which was normalized with total proteins from three independent experiments. Statistics was conducted using multiple t test. E, NELFB-AID and NELFC-AID MEFs were treated with PBS or 0.5 mM IAA and then harvested at different time points. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein and indicated below the corresponding protein. Representative images were shown from three independent repeats. F and G, violin plot distributions of Pol II ChIP-seq reads at the TSS (−0.5 to +0.5kb) and GB (+0.5 to +2.5 kb) in NELFB- AID cells (F) and NELFC-AID cells (G) following treatment of PBS or 0.5 mM IAA for 6 h. Pol II ChIP-seq was from two independent experiments. H, NELFB-AID in MDA-MB-231 cells following IAA treatment. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein Three independent clones were used for the experiment. I, NELFB-AID cell lines that stably expressed EV, WT, or MT194 were treated with IAA. Cell

    Journal: The Journal of biological chemistry

    Article Title: An essential signaling function of cytoplasmic NELFB is independent of RNA polymerase II pausing.

    doi: 10.1016/j.jbc.2023.105259

    Figure Lengend Snippet: Figure 6. NELFB supports progrowth signaling transduction. A, Western blotting of cell lysates from MEFs depleted of NELFB by Cre-loxP. Representative results from three independent repeats. Asterisks indicate the reduced intensity of phosphorylated proteins. B–D, quantification of phosphorylation of various signaling molecules, which was normalized with total proteins from three independent experiments. Statistics was conducted using multiple t test. E, NELFB-AID and NELFC-AID MEFs were treated with PBS or 0.5 mM IAA and then harvested at different time points. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein and indicated below the corresponding protein. Representative images were shown from three independent repeats. F and G, violin plot distributions of Pol II ChIP-seq reads at the TSS (−0.5 to +0.5kb) and GB (+0.5 to +2.5 kb) in NELFB- AID cells (F) and NELFC-AID cells (G) following treatment of PBS or 0.5 mM IAA for 6 h. Pol II ChIP-seq was from two independent experiments. H, NELFB-AID in MDA-MB-231 cells following IAA treatment. Cell lysates were analyzed by Western blotting. The intensity of phosphorylation was normalized with total protein Three independent clones were used for the experiment. I, NELFB-AID cell lines that stably expressed EV, WT, or MT194 were treated with IAA. Cell

    Article Snippet: C-terminal mini-AID– tagged mouse NELFB and human NELFC were cloned into pLenti-6.3/V5-DEST-GFP (Addgene: 40125).

    Techniques: Transduction, Western Blot, Phospho-proteomics, ChIP-sequencing, Clone Assay, Stable Transfection