nb100-221 Search Results


anti nbs1 antibody  (Novus Biologicals)
92
Novus Biologicals anti nbs1 antibody
Anti Nbs1 Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti nbs1 antibody/product/Novus Biologicals
Average 92 stars, based on 1 article reviews
anti nbs1 antibody - by Bioz Stars, 2026-05
92/100 stars
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nbs1  (Novus Biologicals)
92
Novus Biologicals nbs1
FIG. 2. Localization of the <t>Nbs1</t> binding domain in Mdm2. (A) Schematic diagrams of HA-tagged wild-type (WT) Mdm2 and deletion mutants (amino acids indicated). Boxed areas represent domains that bind p53, Nbs1, and ARF or represent the E3 ubiquitin ligase ring domain (RD). The black boxes represent the locations of the nuclear localization signal, nuclear export signal, and nucleolar localization signal from the N terminus to the C terminus, respectively. Mdm2 mutants that did () or did not () coimmunoprecipitate (Co-IP) Nbs1 are indicated. (B) Whole-cell lysates from 293T cells expressing empty vector (Vec) or vectors encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 deletion mutants were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for HA and Nbs1. The location of immunoglobulin heavy chain (IgH) is indicated. (C) Alignment of the amino acids of the Nbs1 binding region of Mdm2 from the organisms indicated. Underlined, italic letters and asterisks indicate amino acid positions where alanine substitutions were made. Xenopus indicates Xenopus laevis. (D to F) 293T cells were transiently transfected with empty vector, a vector encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 point mutants (having two [2 mut], five [5 mut], seven [7 mut], or nine [9 mut] point mutations) and cotransfected with a vector encoding p19ARF (E) or ubiquitin (F). (D and E) Whole-cell lysates were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for proteins indicated to the left of each panel. (F) Whole-cell lysates were Western blotted for p53 and Mdm2.
Nbs1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/nbs1/product/Novus Biologicals
Average 92 stars, based on 1 article reviews
nbs1 - by Bioz Stars, 2026-05
92/100 stars
  Buy from Supplier
anti srebp1 antibody  (Novus Biologicals)
94
Novus Biologicals anti srebp1 antibody
FIG. 2. Localization of the <t>Nbs1</t> binding domain in Mdm2. (A) Schematic diagrams of HA-tagged wild-type (WT) Mdm2 and deletion mutants (amino acids indicated). Boxed areas represent domains that bind p53, Nbs1, and ARF or represent the E3 ubiquitin ligase ring domain (RD). The black boxes represent the locations of the nuclear localization signal, nuclear export signal, and nucleolar localization signal from the N terminus to the C terminus, respectively. Mdm2 mutants that did () or did not () coimmunoprecipitate (Co-IP) Nbs1 are indicated. (B) Whole-cell lysates from 293T cells expressing empty vector (Vec) or vectors encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 deletion mutants were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for HA and Nbs1. The location of immunoglobulin heavy chain (IgH) is indicated. (C) Alignment of the amino acids of the Nbs1 binding region of Mdm2 from the organisms indicated. Underlined, italic letters and asterisks indicate amino acid positions where alanine substitutions were made. Xenopus indicates Xenopus laevis. (D to F) 293T cells were transiently transfected with empty vector, a vector encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 point mutants (having two [2 mut], five [5 mut], seven [7 mut], or nine [9 mut] point mutations) and cotransfected with a vector encoding p19ARF (E) or ubiquitin (F). (D and E) Whole-cell lysates were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for proteins indicated to the left of each panel. (F) Whole-cell lysates were Western blotted for p53 and Mdm2.
Anti Srebp1 Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti srebp1 antibody/product/Novus Biologicals
Average 94 stars, based on 1 article reviews
anti srebp1 antibody - by Bioz Stars, 2026-05
94/100 stars
  Buy from Supplier

Image Search Results


FIG. 2. Localization of the Nbs1 binding domain in Mdm2. (A) Schematic diagrams of HA-tagged wild-type (WT) Mdm2 and deletion mutants (amino acids indicated). Boxed areas represent domains that bind p53, Nbs1, and ARF or represent the E3 ubiquitin ligase ring domain (RD). The black boxes represent the locations of the nuclear localization signal, nuclear export signal, and nucleolar localization signal from the N terminus to the C terminus, respectively. Mdm2 mutants that did () or did not () coimmunoprecipitate (Co-IP) Nbs1 are indicated. (B) Whole-cell lysates from 293T cells expressing empty vector (Vec) or vectors encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 deletion mutants were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for HA and Nbs1. The location of immunoglobulin heavy chain (IgH) is indicated. (C) Alignment of the amino acids of the Nbs1 binding region of Mdm2 from the organisms indicated. Underlined, italic letters and asterisks indicate amino acid positions where alanine substitutions were made. Xenopus indicates Xenopus laevis. (D to F) 293T cells were transiently transfected with empty vector, a vector encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 point mutants (having two [2 mut], five [5 mut], seven [7 mut], or nine [9 mut] point mutations) and cotransfected with a vector encoding p19ARF (E) or ubiquitin (F). (D and E) Whole-cell lysates were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for proteins indicated to the left of each panel. (F) Whole-cell lysates were Western blotted for p53 and Mdm2.

Journal: Molecular and Cellular Biology

Article Title: Mdm2 Promotes Genetic Instability and Transformation Independent of p53

doi: 10.1128/mcb.01584-07

Figure Lengend Snippet: FIG. 2. Localization of the Nbs1 binding domain in Mdm2. (A) Schematic diagrams of HA-tagged wild-type (WT) Mdm2 and deletion mutants (amino acids indicated). Boxed areas represent domains that bind p53, Nbs1, and ARF or represent the E3 ubiquitin ligase ring domain (RD). The black boxes represent the locations of the nuclear localization signal, nuclear export signal, and nucleolar localization signal from the N terminus to the C terminus, respectively. Mdm2 mutants that did () or did not () coimmunoprecipitate (Co-IP) Nbs1 are indicated. (B) Whole-cell lysates from 293T cells expressing empty vector (Vec) or vectors encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 deletion mutants were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for HA and Nbs1. The location of immunoglobulin heavy chain (IgH) is indicated. (C) Alignment of the amino acids of the Nbs1 binding region of Mdm2 from the organisms indicated. Underlined, italic letters and asterisks indicate amino acid positions where alanine substitutions were made. Xenopus indicates Xenopus laevis. (D to F) 293T cells were transiently transfected with empty vector, a vector encoding HA-tagged wild-type Mdm2 (Mdm2) or the indicated Mdm2 point mutants (having two [2 mut], five [5 mut], seven [7 mut], or nine [9 mut] point mutations) and cotransfected with a vector encoding p19ARF (E) or ubiquitin (F). (D and E) Whole-cell lysates were immunoprecipitated with anti-HA (HA IP) and Western blotted with antibodies specific for proteins indicated to the left of each panel. (F) Whole-cell lysates were Western blotted for p53 and Mdm2.

Article Snippet: Following incubation with antibodies against -H2AX (JBW 301; Upstate), Nbs1 (catalog no. 100-143; Novus), or p-S1981-ATM (Rockland), bound antibodies were detected with anti-mouse or anti-rabbit Alexa 594 (Molecular Probes).

Techniques: Binding Assay, Ubiquitin Proteomics, Co-Immunoprecipitation Assay, Expressing, Plasmid Preparation, Immunoprecipitation, Western Blot, Transfection

FIG. 3. The Nbs1 binding domain of Mdm2 is required for inhibi- tion of DNA break repair. p53/ (A), wild-type (B), or ARF/

Journal: Molecular and Cellular Biology

Article Title: Mdm2 Promotes Genetic Instability and Transformation Independent of p53

doi: 10.1128/mcb.01584-07

Figure Lengend Snippet: FIG. 3. The Nbs1 binding domain of Mdm2 is required for inhibi- tion of DNA break repair. p53/ (A), wild-type (B), or ARF/

Article Snippet: Following incubation with antibodies against -H2AX (JBW 301; Upstate), Nbs1 (catalog no. 100-143; Novus), or p-S1981-ATM (Rockland), bound antibodies were detected with anti-mouse or anti-rabbit Alexa 594 (Molecular Probes).

Techniques: Binding Assay

FIG. 4. Mutations in the Nbs1 binding domain of Mdm2 abrogate its ability to inhibit DNA repair. (A to F) Following exposure to 5 Gy of gamma irradiation, p53/ MEFs infected with empty bicistronic GFP-encoding retrovirus or bicistronic retrovirus encoding GFP and wild-type Mdm2 (Mdm2) or Mdm2 with seven (7 mut) or nine (9 mut) point mutations in the Nbs1 binding domain were harvested at the indicated intervals. (A) Comet assays, as described in the legend to Fig. 3, were performed. (B) Equal concentrations of whole-cell lysates were Western blotted with antibodies specific for the proteins indicated to the left of each panel. Phosphorylated H2AX (-H2AX) (C and D) and phosphorylated ATM-S/TQ sites (p-ATM-S/TQ) (E and F) were detected in fixed cells with antibodies specific for each and a fluorescently labeled secondary antibody. The DNA stain DAPI (4 ,6-diamidino-2-phenylindole) was used to visualize the nucleus. Fluorescence was detected by microscopy, and the number of foci per cell was quantified on captured images. Photographs show representative cells. (D and F) Data are the means of three separate experiments, with error bars representing one standard deviation.

Journal: Molecular and Cellular Biology

Article Title: Mdm2 Promotes Genetic Instability and Transformation Independent of p53

doi: 10.1128/mcb.01584-07

Figure Lengend Snippet: FIG. 4. Mutations in the Nbs1 binding domain of Mdm2 abrogate its ability to inhibit DNA repair. (A to F) Following exposure to 5 Gy of gamma irradiation, p53/ MEFs infected with empty bicistronic GFP-encoding retrovirus or bicistronic retrovirus encoding GFP and wild-type Mdm2 (Mdm2) or Mdm2 with seven (7 mut) or nine (9 mut) point mutations in the Nbs1 binding domain were harvested at the indicated intervals. (A) Comet assays, as described in the legend to Fig. 3, were performed. (B) Equal concentrations of whole-cell lysates were Western blotted with antibodies specific for the proteins indicated to the left of each panel. Phosphorylated H2AX (-H2AX) (C and D) and phosphorylated ATM-S/TQ sites (p-ATM-S/TQ) (E and F) were detected in fixed cells with antibodies specific for each and a fluorescently labeled secondary antibody. The DNA stain DAPI (4 ,6-diamidino-2-phenylindole) was used to visualize the nucleus. Fluorescence was detected by microscopy, and the number of foci per cell was quantified on captured images. Photographs show representative cells. (D and F) Data are the means of three separate experiments, with error bars representing one standard deviation.

Article Snippet: Following incubation with antibodies against -H2AX (JBW 301; Upstate), Nbs1 (catalog no. 100-143; Novus), or p-S1981-ATM (Rockland), bound antibodies were detected with anti-mouse or anti-rabbit Alexa 594 (Molecular Probes).

Techniques: Binding Assay, Irradiation, Infection, Western Blot, Labeling, Staining, Fluorescence, Microscopy, Standard Deviation

FIG. 5. Localization of the Mdm2 binding domain in Nbs1. (A) Schematic diagrams of FLAG-tagged wild-type (WT) Nbs1 and Nbs1 deletion mutants (amino acids indicated). The FHA domain, the BRCT domain, and the Mre11 binding domain (Mre11) are labeled. The black boxes indicate nuclear localization signals. FLAG-Nbs1 mutants that did () or did not () coimmunoprecipitate with Mdm2 are indicated. (B) Whole- cell lysates (WCL) and Mdm2 immunoprecipitations (Mdm2 IP) from 293T cells expressing empty vector (Vec) or vectors encoding FLAG-tagged wild-type Nbs1 (Nbs1) or Nbs1 deletion mutants containing the indicated amino acids were Western blotted with antibodies specific for FLAG and Mdm2. The locations of immunoglobulin heavy (IgH) and light (IgL) chains are indicated. (C) Alignment of the Mdm2 binding regions of the Nbs1 proteins from the species indicated. Underlined, italic letters and asterisks indicate amino acid positions where alanine substitutions were made. (D and E) 293T cells with empty vector or vectors encoding FLAG-tagged wild-type Nbs1 (Nbs1) or Nbs1 with four (Mut 4), six (Mut 6), or eight (Mut 8) alanine substitutions in the Mdm2 binding domain. Whole-cell lysates (WCL), Mdm2 immunoprecipitations (Mdm2 IP), and FLAG immunoprecipitations (FLAG IP) were Western blotted with antibodies specified to the left of each panel.

Journal: Molecular and Cellular Biology

Article Title: Mdm2 Promotes Genetic Instability and Transformation Independent of p53

doi: 10.1128/mcb.01584-07

Figure Lengend Snippet: FIG. 5. Localization of the Mdm2 binding domain in Nbs1. (A) Schematic diagrams of FLAG-tagged wild-type (WT) Nbs1 and Nbs1 deletion mutants (amino acids indicated). The FHA domain, the BRCT domain, and the Mre11 binding domain (Mre11) are labeled. The black boxes indicate nuclear localization signals. FLAG-Nbs1 mutants that did () or did not () coimmunoprecipitate with Mdm2 are indicated. (B) Whole- cell lysates (WCL) and Mdm2 immunoprecipitations (Mdm2 IP) from 293T cells expressing empty vector (Vec) or vectors encoding FLAG-tagged wild-type Nbs1 (Nbs1) or Nbs1 deletion mutants containing the indicated amino acids were Western blotted with antibodies specific for FLAG and Mdm2. The locations of immunoglobulin heavy (IgH) and light (IgL) chains are indicated. (C) Alignment of the Mdm2 binding regions of the Nbs1 proteins from the species indicated. Underlined, italic letters and asterisks indicate amino acid positions where alanine substitutions were made. (D and E) 293T cells with empty vector or vectors encoding FLAG-tagged wild-type Nbs1 (Nbs1) or Nbs1 with four (Mut 4), six (Mut 6), or eight (Mut 8) alanine substitutions in the Mdm2 binding domain. Whole-cell lysates (WCL), Mdm2 immunoprecipitations (Mdm2 IP), and FLAG immunoprecipitations (FLAG IP) were Western blotted with antibodies specified to the left of each panel.

Article Snippet: Following incubation with antibodies against -H2AX (JBW 301; Upstate), Nbs1 (catalog no. 100-143; Novus), or p-S1981-ATM (Rockland), bound antibodies were detected with anti-mouse or anti-rabbit Alexa 594 (Molecular Probes).

Techniques: Binding Assay, Labeling, Expressing, Plasmid Preparation, Western Blot

FIG. 6. Wild-type Nbs1 and ATM are necessary for Mdm2-mediated inhibition of DNA break repair. (A) Wild-type (Nbs1/) and Nbs1B/B

Journal: Molecular and Cellular Biology

Article Title: Mdm2 Promotes Genetic Instability and Transformation Independent of p53

doi: 10.1128/mcb.01584-07

Figure Lengend Snippet: FIG. 6. Wild-type Nbs1 and ATM are necessary for Mdm2-mediated inhibition of DNA break repair. (A) Wild-type (Nbs1/) and Nbs1B/B

Article Snippet: Following incubation with antibodies against -H2AX (JBW 301; Upstate), Nbs1 (catalog no. 100-143; Novus), or p-S1981-ATM (Rockland), bound antibodies were detected with anti-mouse or anti-rabbit Alexa 594 (Molecular Probes).

Techniques: Inhibition

FIG. 7. Mdm2 promotes genome instability and transformation in- dependent of p53. (A to C) p53/ MEFs were infected with empty bicistronic GFP-encoding retrovirus (Vector) or bicistronic retrovirus encoding GFP and wild-type Mdm2 (Mdm2) or Mdm2 with nine point mutations in the Nbs1 binding domain (9 mut). (A) Equal concentra- tions of whole-cell lysates were Western blotted for Mdm2 and -actin. (B) Metaphase cells were evaluated for chromosome and chromatid breaks. The total numbers of metaphases assessed per sample are indicated in each bar. Significant differences by Fisher’s exact test are indicated (*, P 0.030; **, P 0.048). (C) Soft agar assays were performed with six identical samples of each, and colonies were counted from all six. Means of each are presented, and error bars represent one standard deviation. Data are representative of four independent experiments. Significant differences by the t test are indicated (*, P 0.00000006; **, P 0.00001).

Journal: Molecular and Cellular Biology

Article Title: Mdm2 Promotes Genetic Instability and Transformation Independent of p53

doi: 10.1128/mcb.01584-07

Figure Lengend Snippet: FIG. 7. Mdm2 promotes genome instability and transformation in- dependent of p53. (A to C) p53/ MEFs were infected with empty bicistronic GFP-encoding retrovirus (Vector) or bicistronic retrovirus encoding GFP and wild-type Mdm2 (Mdm2) or Mdm2 with nine point mutations in the Nbs1 binding domain (9 mut). (A) Equal concentra- tions of whole-cell lysates were Western blotted for Mdm2 and -actin. (B) Metaphase cells were evaluated for chromosome and chromatid breaks. The total numbers of metaphases assessed per sample are indicated in each bar. Significant differences by Fisher’s exact test are indicated (*, P 0.030; **, P 0.048). (C) Soft agar assays were performed with six identical samples of each, and colonies were counted from all six. Means of each are presented, and error bars represent one standard deviation. Data are representative of four independent experiments. Significant differences by the t test are indicated (*, P 0.00000006; **, P 0.00001).

Article Snippet: Following incubation with antibodies against -H2AX (JBW 301; Upstate), Nbs1 (catalog no. 100-143; Novus), or p-S1981-ATM (Rockland), bound antibodies were detected with anti-mouse or anti-rabbit Alexa 594 (Molecular Probes).

Techniques: Transformation Assay, Infection, Plasmid Preparation, Binding Assay, Western Blot, Standard Deviation