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gene exp nsmf mm00480341 m1  (Thermo Fisher)


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    Structured Review

    Thermo Fisher gene exp nsmf mm00480341 m1
    Amino acid alignment of human <t>NELF</t> (NP_056352) and rat Jacob (AJ293697) using CLUSTAL 2.0.11 is shown. The locations of the myristoylation site (brackets above amino acids 1-7) and bipartite NLS of NELF (bold line above amino acids 243-260 of NELF) corresponding to the identical sequence in Jacob protein shaded in aqua). Included in the NLS is the sequence RRKR (mutated to AAKA—the 3A mutant) and adjacent to NLS is the RK sequence (mutated to AA—the 2A mutant), both shaded in magenta. In addition, the peptide sequence used to generate the anti-NELF antibody by Kramer et al [Kramer and Wray 2000] is shown (underline beginning at NELF amino acid 360) and the C-terminal location for our new anti-NELF antibody (boxed sequence at the very C-terminus), which was used for all figures in the current study. Shown, shaded in yellow, are potential sites of phosphorylation of the Jacob protein [Dieterich et al. 2008].
    Gene Exp Nsmf Mm00480341 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nelfb+gene+coding+sequence/Gene+Exp%2E+Nsmf%2C+Mm00480341_m1/pmc03437992-83-71-67
    Average 86 stars, based on 1 article reviews
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    Images

    1) Product Images from "NELF Is a Nuclear Protein Involved in Hypothalamic GnRH Neuronal Migration"

    Article Title: NELF Is a Nuclear Protein Involved in Hypothalamic GnRH Neuronal Migration

    Journal:

    doi: 10.1016/j.mce.2009.11.016

    Amino acid alignment of human NELF (NP_056352) and rat Jacob (AJ293697) using CLUSTAL 2.0.11 is shown. The locations of the myristoylation site (brackets above amino acids 1-7) and bipartite NLS of NELF (bold line above amino acids 243-260 of NELF) corresponding to the identical sequence in Jacob protein shaded in aqua). Included in the NLS is the sequence RRKR (mutated to AAKA—the 3A mutant) and adjacent to NLS is the RK sequence (mutated to AA—the 2A mutant), both shaded in magenta. In addition, the peptide sequence used to generate the anti-NELF antibody by Kramer et al [Kramer and Wray 2000] is shown (underline beginning at NELF amino acid 360) and the C-terminal location for our new anti-NELF antibody (boxed sequence at the very C-terminus), which was used for all figures in the current study. Shown, shaded in yellow, are potential sites of phosphorylation of the Jacob protein [Dieterich et al. 2008].
    Figure Legend Snippet: Amino acid alignment of human NELF (NP_056352) and rat Jacob (AJ293697) using CLUSTAL 2.0.11 is shown. The locations of the myristoylation site (brackets above amino acids 1-7) and bipartite NLS of NELF (bold line above amino acids 243-260 of NELF) corresponding to the identical sequence in Jacob protein shaded in aqua). Included in the NLS is the sequence RRKR (mutated to AAKA—the 3A mutant) and adjacent to NLS is the RK sequence (mutated to AA—the 2A mutant), both shaded in magenta. In addition, the peptide sequence used to generate the anti-NELF antibody by Kramer et al [Kramer and Wray 2000] is shown (underline beginning at NELF amino acid 360) and the C-terminal location for our new anti-NELF antibody (boxed sequence at the very C-terminus), which was used for all figures in the current study. Shown, shaded in yellow, are potential sites of phosphorylation of the Jacob protein [Dieterich et al. 2008].

    Techniques Used: Sequencing, Mutagenesis

    A) Northern blot analysis with a 32P labeled human NELF cDNA probe. Although not well see in the figure, low expression levels were observed in the small intestine, skeletal muscle, and peripheral WBCs. B) QRT-PCR of mouse Nelf mRNA expression in each of the three neuronal GnRH cell lines. Triplicate experiments (n=9 for each cell line) showed that all three GnRH cell lines express Nelf, but levels were not significantly different among cell lines. C) QRT-PCR of mouse Nelf mRNA expression following exogenous GnRH agonist treatment in LβT2 pituitary cells (n=3/group). Nelf expression increased three-fold at three hours, while Chd7 expression did not change after GnRH agonist treatment. Nelf expression was greater at both 3 and 12 hr vs. control (P<0.001). Although there was a statistically significant rise in Chd7 expression at 3 hr, this effect is only ~ 40% increase over baseline, questioning any biological significance.
    Figure Legend Snippet: A) Northern blot analysis with a 32P labeled human NELF cDNA probe. Although not well see in the figure, low expression levels were observed in the small intestine, skeletal muscle, and peripheral WBCs. B) QRT-PCR of mouse Nelf mRNA expression in each of the three neuronal GnRH cell lines. Triplicate experiments (n=9 for each cell line) showed that all three GnRH cell lines express Nelf, but levels were not significantly different among cell lines. C) QRT-PCR of mouse Nelf mRNA expression following exogenous GnRH agonist treatment in LβT2 pituitary cells (n=3/group). Nelf expression increased three-fold at three hours, while Chd7 expression did not change after GnRH agonist treatment. Nelf expression was greater at both 3 and 12 hr vs. control (P<0.001). Although there was a statistically significant rise in Chd7 expression at 3 hr, this effect is only ~ 40% increase over baseline, questioning any biological significance.

    Techniques Used: Northern Blot, Labeling, Expressing, Quantitative RT-PCR

    A) Protein expression by western blot analysis with our new anti-NELF antibody is greater in migratory NLT and GN11 cells than postmigratory GT1-7 cells. B) Following cellular fractionation, NELF expression is greater in the nucleus than the cytoplasm in all three GnRH cell lines as represented by a ~63 kDa band. A smaller ~57kDa nonspecific band was seen in the nuclear fraction, which could represent a NELF splice variant. Note absence of the 63 kDa band in COS-7 cells. The lower figure clearly shows greater nuclear expression in all three GnRH cell lines. Beta-actin was used as a loading control. C) Following sucrose density gradient separation, NELF expression was seen in the nucleus. The most intense expression of NELF was seen in the final nuclear pellet P2. Abbreviations are as follows: H = histone; S1 = supernatant 1; P = pellet 1; 1.6 M and 1.9 M sucrose layers; P2 = pellet 2, which comprises the nuclear pellet. A 100 kDa nonspecific band is seen in some fractions.
    Figure Legend Snippet: A) Protein expression by western blot analysis with our new anti-NELF antibody is greater in migratory NLT and GN11 cells than postmigratory GT1-7 cells. B) Following cellular fractionation, NELF expression is greater in the nucleus than the cytoplasm in all three GnRH cell lines as represented by a ~63 kDa band. A smaller ~57kDa nonspecific band was seen in the nuclear fraction, which could represent a NELF splice variant. Note absence of the 63 kDa band in COS-7 cells. The lower figure clearly shows greater nuclear expression in all three GnRH cell lines. Beta-actin was used as a loading control. C) Following sucrose density gradient separation, NELF expression was seen in the nucleus. The most intense expression of NELF was seen in the final nuclear pellet P2. Abbreviations are as follows: H = histone; S1 = supernatant 1; P = pellet 1; 1.6 M and 1.9 M sucrose layers; P2 = pellet 2, which comprises the nuclear pellet. A 100 kDa nonspecific band is seen in some fractions.

    Techniques Used: Expressing, Western Blot, Cell Fractionation, Variant Assay

    A) Immunofluorescence with confocal microscopy (63X) demonstrates predominant NELF expression in the nucleus in all three cell lines, as shown by DAPI and anti-NELF antibody staining. As a negative control, peptide used to generate the antibody was preincubated with the antibody, and no NELF staining was seen (not shown). B) Western blot analysis of the exogenous NELF/GFP fusion product in NLT cells is shown. The expected 93kDa band is shown using both anti-NELF and anti-GFP antibodies. Beta-actin is the loading control. C) Nuclear/cytoplasmic (N/C) ratios for wild type and 3A NELF mutant in NLT cells are shown. In the inset, immunofluorescence demonstrates nuclear GFP staining in the wild type, but diffuse staining in the 3A mutant, consistent with its reduced nuclear/cytoplasmic expression.
    Figure Legend Snippet: A) Immunofluorescence with confocal microscopy (63X) demonstrates predominant NELF expression in the nucleus in all three cell lines, as shown by DAPI and anti-NELF antibody staining. As a negative control, peptide used to generate the antibody was preincubated with the antibody, and no NELF staining was seen (not shown). B) Western blot analysis of the exogenous NELF/GFP fusion product in NLT cells is shown. The expected 93kDa band is shown using both anti-NELF and anti-GFP antibodies. Beta-actin is the loading control. C) Nuclear/cytoplasmic (N/C) ratios for wild type and 3A NELF mutant in NLT cells are shown. In the inset, immunofluorescence demonstrates nuclear GFP staining in the wild type, but diffuse staining in the 3A mutant, consistent with its reduced nuclear/cytoplasmic expression.

    Techniques Used: Immunofluorescence, Confocal Microscopy, Expressing, Staining, Negative Control, Western Blot, Mutagenesis

    Boyden chamber NLT cell migration results are shown. On the left, NELF knockdown (KD) results in a three-fold reduction in migration compared with the control. On the right, when fluorescence-activated cell sorting (FACS) was done to enrich for transfected cells, GnRH neuron migration was reduced more than 12-fold.
    Figure Legend Snippet: Boyden chamber NLT cell migration results are shown. On the left, NELF knockdown (KD) results in a three-fold reduction in migration compared with the control. On the right, when fluorescence-activated cell sorting (FACS) was done to enrich for transfected cells, GnRH neuron migration was reduced more than 12-fold.

    Techniques Used: Migration, Fluorescence, FACS, Transfection

    Schematic presentation of putative zinc finger domains of NELF are shown. Two zinc finger domains with HH-CC and CH-HC consensus are shown consecutively. These zinc finger domains were represented in the Pfam program of PF08080 (http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF08080) and PF09337 (http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF09337). Red colored circles represent cysteine or histidine residues binding directly with zinc ions. The alignment of NELF proteins containing two putative zinc finger domains from five different species of human, mouse, rat, chicken and zebrafish. The fully conserved putative zinc finger domains of HH-CC and CH-HC are boxed in red.
    Figure Legend Snippet: Schematic presentation of putative zinc finger domains of NELF are shown. Two zinc finger domains with HH-CC and CH-HC consensus are shown consecutively. These zinc finger domains were represented in the Pfam program of PF08080 (http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF08080) and PF09337 (http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF09337). Red colored circles represent cysteine or histidine residues binding directly with zinc ions. The alignment of NELF proteins containing two putative zinc finger domains from five different species of human, mouse, rat, chicken and zebrafish. The fully conserved putative zinc finger domains of HH-CC and CH-HC are boxed in red.

    Techniques Used: Binding Assay



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    Image Search Results


    a , b Percentages of CD62L + CD45RA + cells within CD4 + ( a ) and CD8 + ( b ) populations of 28z or 28z-hNELFB CAR-T cells after 10 days of in vitro expansion, n = 4/group. c Survival curves of Raji tumor-bearing mice receiving PBS or mock T cells, CD19 CAR-28z T cells, or CD19 CAR-28z-hNELFB T cells. d Model of enhancer–promoter looping mediated by NELFB, Pol II, and TCF1. Mean differences were compared using Student’s t -test. Log-rank (Mantel–Cox) tests were used for survival analyses. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: RNA polymerase II pausing factor NELF in CD8 + T cells promotes antitumor immunity

    doi: 10.1038/s41467-022-29869-2

    Figure Lengend Snippet: a , b Percentages of CD62L + CD45RA + cells within CD4 + ( a ) and CD8 + ( b ) populations of 28z or 28z-hNELFB CAR-T cells after 10 days of in vitro expansion, n = 4/group. c Survival curves of Raji tumor-bearing mice receiving PBS or mock T cells, CD19 CAR-28z T cells, or CD19 CAR-28z-hNELFB T cells. d Model of enhancer–promoter looping mediated by NELFB, Pol II, and TCF1. Mean differences were compared using Student’s t -test. Log-rank (Mantel–Cox) tests were used for survival analyses. Source data are provided as a Source Data file.

    Article Snippet: The human NELFB gene coding sequence was inserted downstream of the CAR19-28z-encoding sequence, with the P2A cleavage sequence in between (Gene Universal, Inc.).

    Techniques: In Vitro