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    Biomol GmbH recombinant full length human sirt1
    <t>SIRT1</t> is phosphorylated by JNK1. A , Schematic representation of full length human SIRT1 (FL hSIRT1) protein and a truncated form (aa 170–701 hSIRT1). Triangles show putative JNK1 phosphorylation sites. B , phosphorylation of SIRT1 by recombinant JNK1. FL hSIRT1 or a.a. 170–701 hSIRT1 was incubated with recombinant JNK1 or GSK3β in the presence of γ-[ 32 P]-ATP. C , Schematic representation of mouse SIRT1 GST fragments. Triangle represents the putative JNK phosphorylation site. D, In vitro phosphorylation of mouse SIRT1 GST when treated with JNK1 immunoprecipitates from anisomycin-treated C2C12 cells or recombinant JNK1. Truncated hSIRT1 (a.a. 170–701 hSIRT1) was used as positive control.
    Recombinant Full Length Human Sirt1, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant full length human sirt1/product/Biomol GmbH
    Average 85 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    recombinant full length human sirt1 - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

    89
    Addgene inc human full length human sirt1
    <t>Sirt1</t> protects neuronal cells from HA and Aβ-induced PGC1α suppression and cytotoxicity. ( A ) Western blotting assays showed the co-treatment of HA and Aβ inhibits expressions of Sirt1 and PGC1α. However, the addition of Salubrinal (50 μM) significantly blocked these inhibitions; ( B ) Sirt1 over-expression significantly restores HA and Aβ-inhibited PGC1α levels, ( C ) and contributes to a better survival rate in HA and Aβ co-treated cells; ( D ) Sirt1 over-expression failed to inhibit the levels of p-Thr980 PERK and p-Ser51 eIF2α in HA and Aβ co-treated cells, indicating that ER stress occurs upstream of Sirt1 down-regulation. All results are shown from three independent experiments, and values are presented as mean ± SEM. Significant differences were determined by using multiple comparisons of Dunnett’s post-hoc test for ** p
    Human Full Length Human Sirt1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 89/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human full length human sirt1/product/Addgene inc
    Average 89 stars, based on 63 article reviews
    Price from $9.99 to $1999.99
    human full length human sirt1 - by Bioz Stars, 2020-09
    89/100 stars
      Buy from Supplier

    Image Search Results


    SIRT1 is phosphorylated by JNK1. A , Schematic representation of full length human SIRT1 (FL hSIRT1) protein and a truncated form (aa 170–701 hSIRT1). Triangles show putative JNK1 phosphorylation sites. B , phosphorylation of SIRT1 by recombinant JNK1. FL hSIRT1 or a.a. 170–701 hSIRT1 was incubated with recombinant JNK1 or GSK3β in the presence of γ-[ 32 P]-ATP. C , Schematic representation of mouse SIRT1 GST fragments. Triangle represents the putative JNK phosphorylation site. D, In vitro phosphorylation of mouse SIRT1 GST when treated with JNK1 immunoprecipitates from anisomycin-treated C2C12 cells or recombinant JNK1. Truncated hSIRT1 (a.a. 170–701 hSIRT1) was used as positive control.

    Journal: PLoS ONE

    Article Title: JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

    doi: 10.1371/journal.pone.0008414

    Figure Lengend Snippet: SIRT1 is phosphorylated by JNK1. A , Schematic representation of full length human SIRT1 (FL hSIRT1) protein and a truncated form (aa 170–701 hSIRT1). Triangles show putative JNK1 phosphorylation sites. B , phosphorylation of SIRT1 by recombinant JNK1. FL hSIRT1 or a.a. 170–701 hSIRT1 was incubated with recombinant JNK1 or GSK3β in the presence of γ-[ 32 P]-ATP. C , Schematic representation of mouse SIRT1 GST fragments. Triangle represents the putative JNK phosphorylation site. D, In vitro phosphorylation of mouse SIRT1 GST when treated with JNK1 immunoprecipitates from anisomycin-treated C2C12 cells or recombinant JNK1. Truncated hSIRT1 (a.a. 170–701 hSIRT1) was used as positive control.

    Article Snippet: SIRT1 Recombinant Protein Purification For in vitro kinase studies, recombinant full-length human SIRT1 (FL hSIRT1) was purchased from Biomol International, LP (Plymouth Meeting, PA).

    Techniques: Recombinant, Incubation, In Vitro, Positive Control

    SIRT1 does not regulate JNK1 phosphorylation or activity. A , Inhibition of SIRT1 activity by nicotinamide or Sirtinol does not affect phosphorylation of JNK1 in response to anisomycin. B , Inhibition of SIRT1 activity by nicotinamide or Sirtinol does not affect activity of JNK1 in response to anisomycin. JNK1 activity was measured by its ability to phosphorylate c-Jun. C , Knockdown of SIRT1 by siRNA does not affect anisomycin-mediated phosphorylation of JNK1. D , Knockdown of SIRT1 does not affect anisomycin-stimulated activity of JNK1. Clear bars are control. Black bars are SIRT1 knockdown.

    Journal: PLoS ONE

    Article Title: JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

    doi: 10.1371/journal.pone.0008414

    Figure Lengend Snippet: SIRT1 does not regulate JNK1 phosphorylation or activity. A , Inhibition of SIRT1 activity by nicotinamide or Sirtinol does not affect phosphorylation of JNK1 in response to anisomycin. B , Inhibition of SIRT1 activity by nicotinamide or Sirtinol does not affect activity of JNK1 in response to anisomycin. JNK1 activity was measured by its ability to phosphorylate c-Jun. C , Knockdown of SIRT1 by siRNA does not affect anisomycin-mediated phosphorylation of JNK1. D , Knockdown of SIRT1 does not affect anisomycin-stimulated activity of JNK1. Clear bars are control. Black bars are SIRT1 knockdown.

    Article Snippet: SIRT1 Recombinant Protein Purification For in vitro kinase studies, recombinant full-length human SIRT1 (FL hSIRT1) was purchased from Biomol International, LP (Plymouth Meeting, PA).

    Techniques: Activity Assay, Inhibition

    SIRT1 and JNK1 interact. A , Coimmunoprecipitation of SIRT1 with total JNK1 and phospho-JNK1 after treatment with anisomycin or H 2 O 2 . Anisomycin and H 2 O 2 cause phosphorylation of JNK1 and interaction with SIRT1. B , Coimmunoprecipitation of SIRT1 with either total JNK1 or phospho-JNK1 from HEK293 cell lysates. SIRT1 immunoprecipitated specifically with phospho-JNK1 in response to anisomycin. C , Coimmunoprecipitation of SIRT1 with either total JNK1 plus phospho-JNK1 or phospho-JNK1 from C2C12 cell lysates. SIRT1 immunoprecipitated with phospho-JNK1 in response to anisomycin or H 2 O 2 .

    Journal: PLoS ONE

    Article Title: JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

    doi: 10.1371/journal.pone.0008414

    Figure Lengend Snippet: SIRT1 and JNK1 interact. A , Coimmunoprecipitation of SIRT1 with total JNK1 and phospho-JNK1 after treatment with anisomycin or H 2 O 2 . Anisomycin and H 2 O 2 cause phosphorylation of JNK1 and interaction with SIRT1. B , Coimmunoprecipitation of SIRT1 with either total JNK1 or phospho-JNK1 from HEK293 cell lysates. SIRT1 immunoprecipitated specifically with phospho-JNK1 in response to anisomycin. C , Coimmunoprecipitation of SIRT1 with either total JNK1 plus phospho-JNK1 or phospho-JNK1 from C2C12 cell lysates. SIRT1 immunoprecipitated with phospho-JNK1 in response to anisomycin or H 2 O 2 .

    Article Snippet: SIRT1 Recombinant Protein Purification For in vitro kinase studies, recombinant full-length human SIRT1 (FL hSIRT1) was purchased from Biomol International, LP (Plymouth Meeting, PA).

    Techniques: Immunoprecipitation

    JNK1 regulates cellular localization of SIRT1. Immunohistochemistry of SIRT1 and JNK1. Cells were treated with control ( A ), H 2 O 2 ( B ), JNKi ( C ) or H 2 O 2 plus JNKi ( D ). Cellular localization of JNK1 was determined by anti-rabbit JNK antibody and SIRT1 by anti-mouse SIRT1 antibody. Cells were stained with DAPI stain to visualize nuclei. Arrows show SIRT1 localization.

    Journal: PLoS ONE

    Article Title: JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

    doi: 10.1371/journal.pone.0008414

    Figure Lengend Snippet: JNK1 regulates cellular localization of SIRT1. Immunohistochemistry of SIRT1 and JNK1. Cells were treated with control ( A ), H 2 O 2 ( B ), JNKi ( C ) or H 2 O 2 plus JNKi ( D ). Cellular localization of JNK1 was determined by anti-rabbit JNK antibody and SIRT1 by anti-mouse SIRT1 antibody. Cells were stained with DAPI stain to visualize nuclei. Arrows show SIRT1 localization.

    Article Snippet: SIRT1 Recombinant Protein Purification For in vitro kinase studies, recombinant full-length human SIRT1 (FL hSIRT1) was purchased from Biomol International, LP (Plymouth Meeting, PA).

    Techniques: Immunohistochemistry, Staining

    Mutation of putative JNK phosphorylation sites on hSIRT1 reduces phosphorylation and activity of SIRT1. A , In vitro phosphorylation of full length (FL) hSIRT1 or SIRT1 with the putative JNK phosphorylation sites mutated (Mt-SIRT1). FL hSIRT1 or Mt-SIRT1 was incubated with recombinant JNK1. B , Mt-SIRT1 shows decreased activity in deacetylation of histone H3. Cells were transfected with the empty vector (CMV), WT hSIRT1 (WT) or Mt-SIRT1 (Mt) then treated with H 2 O 2 or H 2 O 2 plus JNK inhibitor (JNKi). SIRT1, acetylated histone H3 (Ac-H3) or total histone H3 were examined by Western blotting. C , Mt-SIRT1 shows similar activity to WT SIRT1 in deacetylation of p53. Experiment performed as in B , except that acetylated p53 (Ac-p53) and total p53 levels were monitored. The ratio Ac/Total shows the quantification of the expression levels of the acetylated substrates vs . the total levels of the same substrates. D , Mt-SIRT1 shows decreased activity in deacetylation of histone3 (H3). Cells were transfected with the empty vector (CMV), WT hSIRT1 (WT) or Mt-SIRT1 (Mt) then treated with anisomycin or anisomycin plus JNK inhibitor (JNKi). SIRT1, acetylated histone H3 or total H3 were examined by Western blotting. E , Mt-SIRT1 shows similar activity to WT SIRT1 in deacetylation of p53 when cells were treated with anisomycin. The experiment was performed as in D , and the levels of acetylated p53 (Ac-p53) and total p53 were determined by Western blotting.

    Journal: PLoS ONE

    Article Title: JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

    doi: 10.1371/journal.pone.0008414

    Figure Lengend Snippet: Mutation of putative JNK phosphorylation sites on hSIRT1 reduces phosphorylation and activity of SIRT1. A , In vitro phosphorylation of full length (FL) hSIRT1 or SIRT1 with the putative JNK phosphorylation sites mutated (Mt-SIRT1). FL hSIRT1 or Mt-SIRT1 was incubated with recombinant JNK1. B , Mt-SIRT1 shows decreased activity in deacetylation of histone H3. Cells were transfected with the empty vector (CMV), WT hSIRT1 (WT) or Mt-SIRT1 (Mt) then treated with H 2 O 2 or H 2 O 2 plus JNK inhibitor (JNKi). SIRT1, acetylated histone H3 (Ac-H3) or total histone H3 were examined by Western blotting. C , Mt-SIRT1 shows similar activity to WT SIRT1 in deacetylation of p53. Experiment performed as in B , except that acetylated p53 (Ac-p53) and total p53 levels were monitored. The ratio Ac/Total shows the quantification of the expression levels of the acetylated substrates vs . the total levels of the same substrates. D , Mt-SIRT1 shows decreased activity in deacetylation of histone3 (H3). Cells were transfected with the empty vector (CMV), WT hSIRT1 (WT) or Mt-SIRT1 (Mt) then treated with anisomycin or anisomycin plus JNK inhibitor (JNKi). SIRT1, acetylated histone H3 or total H3 were examined by Western blotting. E , Mt-SIRT1 shows similar activity to WT SIRT1 in deacetylation of p53 when cells were treated with anisomycin. The experiment was performed as in D , and the levels of acetylated p53 (Ac-p53) and total p53 were determined by Western blotting.

    Article Snippet: SIRT1 Recombinant Protein Purification For in vitro kinase studies, recombinant full-length human SIRT1 (FL hSIRT1) was purchased from Biomol International, LP (Plymouth Meeting, PA).

    Techniques: Mutagenesis, Activity Assay, In Vitro, Incubation, Recombinant, Transfection, Plasmid Preparation, Western Blot, Expressing

    Sirt1 protects neuronal cells from HA and Aβ-induced PGC1α suppression and cytotoxicity. ( A ) Western blotting assays showed the co-treatment of HA and Aβ inhibits expressions of Sirt1 and PGC1α. However, the addition of Salubrinal (50 μM) significantly blocked these inhibitions; ( B ) Sirt1 over-expression significantly restores HA and Aβ-inhibited PGC1α levels, ( C ) and contributes to a better survival rate in HA and Aβ co-treated cells; ( D ) Sirt1 over-expression failed to inhibit the levels of p-Thr980 PERK and p-Ser51 eIF2α in HA and Aβ co-treated cells, indicating that ER stress occurs upstream of Sirt1 down-regulation. All results are shown from three independent experiments, and values are presented as mean ± SEM. Significant differences were determined by using multiple comparisons of Dunnett’s post-hoc test for ** p

    Journal: International Journal of Molecular Sciences

    Article Title: Humic Acid Increases Amyloid β-Induced Cytotoxicity by Induction of ER Stress in Human SK-N-MC Neuronal Cells

    doi: 10.3390/ijms160510426

    Figure Lengend Snippet: Sirt1 protects neuronal cells from HA and Aβ-induced PGC1α suppression and cytotoxicity. ( A ) Western blotting assays showed the co-treatment of HA and Aβ inhibits expressions of Sirt1 and PGC1α. However, the addition of Salubrinal (50 μM) significantly blocked these inhibitions; ( B ) Sirt1 over-expression significantly restores HA and Aβ-inhibited PGC1α levels, ( C ) and contributes to a better survival rate in HA and Aβ co-treated cells; ( D ) Sirt1 over-expression failed to inhibit the levels of p-Thr980 PERK and p-Ser51 eIF2α in HA and Aβ co-treated cells, indicating that ER stress occurs upstream of Sirt1 down-regulation. All results are shown from three independent experiments, and values are presented as mean ± SEM. Significant differences were determined by using multiple comparisons of Dunnett’s post-hoc test for ** p

    Article Snippet: Human full-length human Sirt1 was obtained from Addgene (Cambridge, MA, USA) and cloned into a pcDNA3.1 expression vector.

    Techniques: Western Blot, Over Expression