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inactive sirt1 h363y mutant  (Addgene inc)


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    Structured Review

    Addgene inc inactive sirt1 h363y mutant
    <t>SIRT1</t> mediates the regulatory effect of NAD + on primary cilia. (a) <t>SIRT1</t> activator resveratrol (20 μM) treatment elongates cilia length in N1 cells ( n = 8 wells per group). AC3: Adenylyl cyclase 3. (b) Effects of overexpression (OE) of wild–type SIRT1 and its catalytically inactive <t>H363Y</t> mutant on ciliary length in N1 cells ( n = 5 wells per group). (c) Effect of treatment with the SIRT1 inhibitor EX527 (100 μm for 16 h) on NR (100 μM)‐induced cilia growth ( n = 6 wells per group). (d) Sirt1 knockdown with small inhibitory RNA ( siSirt1 ) prevents NMN (100 μM)–induced cilia elongation ( n = 3 wells per group). (e) Effect of SIRT1 OE on mRNA expression levels of multiple cilia‐related genes ( n = 6 wells per group). (f) Sirt1 knockdown inhibits NMN‐induced upregulation of cilia‐related genes ( n = 6 wells per group). (g, h) SIRT1 and RFX1 cooperatively regulate the promoter activity of the Ift88 gene ( n = 3 wells per group). (i, j) Molecular interaction between SIRT1 and RFX1, and SIRT1‐mediated deacetylation of RFX1, demonstrated by sequential immunoprecipitation (IP) and immunoblotting (IB) in N1 cells with or without SIRT1 OE. Ac‐K, acetylated lysine. (k) Effect of autophagy inhibition by Atg5 knockdown or 3‐MA treatment on SIRT1‐induced changes in primary cilia ( n = 5). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t‐ test (a, e), one‐way ANOVA (b, c, f, g, h, k), or two‐way (d) ANOVA with Tukey's post hoc test. n.s., not significant. Scale bars, 20 μm.
    Inactive Sirt1 H363y Mutant, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mutant/Flag-SIRT1+H363Y+(Plasmid+%231792)/pmc13684318-319-13-19
    Average 93 stars, based on 79 article reviews
    inactive sirt1 h363y mutant - by Bioz Stars, 2026-11
    93/100 stars

    Images

    1) Product Images from "A Cilia–Centered Nicotinamide Adenine Dinucleotide ( NAD + ) Signaling Network Regulates Hypothalamic Lysosomal Homeostasis and Metabolic Aging"

    Article Title: A Cilia–Centered Nicotinamide Adenine Dinucleotide ( NAD + ) Signaling Network Regulates Hypothalamic Lysosomal Homeostasis and Metabolic Aging

    Journal: Aging Cell

    doi: 10.1111/acel.70745

    SIRT1 mediates the regulatory effect of NAD + on primary cilia. (a) SIRT1 activator resveratrol (20 μM) treatment elongates cilia length in N1 cells ( n = 8 wells per group). AC3: Adenylyl cyclase 3. (b) Effects of overexpression (OE) of wild–type SIRT1 and its catalytically inactive H363Y mutant on ciliary length in N1 cells ( n = 5 wells per group). (c) Effect of treatment with the SIRT1 inhibitor EX527 (100 μm for 16 h) on NR (100 μM)‐induced cilia growth ( n = 6 wells per group). (d) Sirt1 knockdown with small inhibitory RNA ( siSirt1 ) prevents NMN (100 μM)–induced cilia elongation ( n = 3 wells per group). (e) Effect of SIRT1 OE on mRNA expression levels of multiple cilia‐related genes ( n = 6 wells per group). (f) Sirt1 knockdown inhibits NMN‐induced upregulation of cilia‐related genes ( n = 6 wells per group). (g, h) SIRT1 and RFX1 cooperatively regulate the promoter activity of the Ift88 gene ( n = 3 wells per group). (i, j) Molecular interaction between SIRT1 and RFX1, and SIRT1‐mediated deacetylation of RFX1, demonstrated by sequential immunoprecipitation (IP) and immunoblotting (IB) in N1 cells with or without SIRT1 OE. Ac‐K, acetylated lysine. (k) Effect of autophagy inhibition by Atg5 knockdown or 3‐MA treatment on SIRT1‐induced changes in primary cilia ( n = 5). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t‐ test (a, e), one‐way ANOVA (b, c, f, g, h, k), or two‐way (d) ANOVA with Tukey's post hoc test. n.s., not significant. Scale bars, 20 μm.
    Figure Legend Snippet: SIRT1 mediates the regulatory effect of NAD + on primary cilia. (a) SIRT1 activator resveratrol (20 μM) treatment elongates cilia length in N1 cells ( n = 8 wells per group). AC3: Adenylyl cyclase 3. (b) Effects of overexpression (OE) of wild–type SIRT1 and its catalytically inactive H363Y mutant on ciliary length in N1 cells ( n = 5 wells per group). (c) Effect of treatment with the SIRT1 inhibitor EX527 (100 μm for 16 h) on NR (100 μM)‐induced cilia growth ( n = 6 wells per group). (d) Sirt1 knockdown with small inhibitory RNA ( siSirt1 ) prevents NMN (100 μM)–induced cilia elongation ( n = 3 wells per group). (e) Effect of SIRT1 OE on mRNA expression levels of multiple cilia‐related genes ( n = 6 wells per group). (f) Sirt1 knockdown inhibits NMN‐induced upregulation of cilia‐related genes ( n = 6 wells per group). (g, h) SIRT1 and RFX1 cooperatively regulate the promoter activity of the Ift88 gene ( n = 3 wells per group). (i, j) Molecular interaction between SIRT1 and RFX1, and SIRT1‐mediated deacetylation of RFX1, demonstrated by sequential immunoprecipitation (IP) and immunoblotting (IB) in N1 cells with or without SIRT1 OE. Ac‐K, acetylated lysine. (k) Effect of autophagy inhibition by Atg5 knockdown or 3‐MA treatment on SIRT1‐induced changes in primary cilia ( n = 5). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t‐ test (a, e), one‐way ANOVA (b, c, f, g, h, k), or two‐way (d) ANOVA with Tukey's post hoc test. n.s., not significant. Scale bars, 20 μm.

    Techniques Used: Over Expression, Mutagenesis, Knockdown, Expressing, Activity Assay, Immunoprecipitation, Western Blot, Inhibition

    Primary cilia are essential for NAD + ‐mediated regulation of lysosomal acidity. (a) Effects of NAD + elevation induced by NAD or its precursors (NMN, NR) treatment on lysosomal acidity, assessed by LysoSensor fluorescence intensity ( n = 6 wells per group). Scale bars, 20 μm. (b) Effect of overexpression of wild‐type SIRT1 and a catalytically inactive SIRT1 mutant ( H363Y ) on lysosomal acidity ( n = 5 wells per group). (c, d) Effects of NAD + depletion induced by FK866 treatment or Nampt knockdown on lysosomal acidity ( n = 6 wells per group). Scale bars, 20 μm. (e) Restorative effects of NMN co‐treatment on the FK866‐induced lysosomal deacidification in N1 cells transfected with control siRNA ( siControl ), Ift88 siRNA ( siIft88 ), or Ift20 siRNA ( siIft20 ) ( n = 4 wells per group). Scale bars, 20 μm. (f) Effects of NAD + depletion (FK866) and repletion (FK866 + NMN) on lysosomal cathepsin B activity, assessed by the Magic Red assay, in N1 cells with or without ciliary dysgenesis ( n = 6 wells per group). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t ‐test (c, d), one‐way ANOVA (a, b), or two‐way ANOVA (e, f), followed by Tukey's post hoc test. n.s., not significant.
    Figure Legend Snippet: Primary cilia are essential for NAD + ‐mediated regulation of lysosomal acidity. (a) Effects of NAD + elevation induced by NAD or its precursors (NMN, NR) treatment on lysosomal acidity, assessed by LysoSensor fluorescence intensity ( n = 6 wells per group). Scale bars, 20 μm. (b) Effect of overexpression of wild‐type SIRT1 and a catalytically inactive SIRT1 mutant ( H363Y ) on lysosomal acidity ( n = 5 wells per group). (c, d) Effects of NAD + depletion induced by FK866 treatment or Nampt knockdown on lysosomal acidity ( n = 6 wells per group). Scale bars, 20 μm. (e) Restorative effects of NMN co‐treatment on the FK866‐induced lysosomal deacidification in N1 cells transfected with control siRNA ( siControl ), Ift88 siRNA ( siIft88 ), or Ift20 siRNA ( siIft20 ) ( n = 4 wells per group). Scale bars, 20 μm. (f) Effects of NAD + depletion (FK866) and repletion (FK866 + NMN) on lysosomal cathepsin B activity, assessed by the Magic Red assay, in N1 cells with or without ciliary dysgenesis ( n = 6 wells per group). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t ‐test (c, d), one‐way ANOVA (a, b), or two‐way ANOVA (e, f), followed by Tukey's post hoc test. n.s., not significant.

    Techniques Used: Fluorescence, Over Expression, Mutagenesis, Knockdown, Transfection, Control, Activity Assay

    Related Articles

    Mutagenesis:

    Article Title: Measuring PETase enzyme kinetics by single-molecule microscopy
    Article Snippet: .. DNA plasmids for wild-type PETase (PETase, I. sakaiensis , accession number: A0A0K8P6T7, Addgene number: #112202), hyperactive mutant (Addgene number: #112203) and the impaired mutant (Addgene number: #112204) were purchased from Addgene ( ). .. Plasmids were transformed into E. coli C41(DE3) (Lucigen) and inoculated on a Nutrient Agar plate containing 100 μg/mL ampicillin (VWR; Cas: 69-52-3).

    Article Title: Polymerase-amplified release of ATP (POLARA) for detecting single nucleotide variants in RNA and DNA †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03901a
    Article Snippet: .. Synthesis of RNA Targets For the JAK2 and BRAF genes, PCR was performed on plasmids2–4 containing inserts with the wild-type (JAK2: Addgene plasmid #23915) or mutant (JAK2 V617F: Addgene plasmid #64610) sequence to generate 500mer double-stranded DNA templates. ..

    Article Title: A p53/lnc‐Ip53 Negative Feedback Loop Regulates Tumor Growth and Chemoresistance
    Article Snippet: .. To examine the activity of p53 signaling, cells were transfected with 10 nM silnc-Ip53 or NC duplex for 24 hours, followed by co-transfection of 25 ng pRL-TK and 25 ng firefly luciferase reporter plasmids containing wild-type (PG13-Luc; Addgene Plasmid #16442, Cambridge, MA, USA) or mutant (MG15-Luc; Addgene Plasmid #16443) p53 binding sites upstream of the firefly luciferase gene for another 36 hours. ..

    Polymerase Chain Reaction:

    Article Title: Polymerase-amplified release of ATP (POLARA) for detecting single nucleotide variants in RNA and DNA †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03901a
    Article Snippet: .. Synthesis of RNA Targets For the JAK2 and BRAF genes, PCR was performed on plasmids2–4 containing inserts with the wild-type (JAK2: Addgene plasmid #23915) or mutant (JAK2 V617F: Addgene plasmid #64610) sequence to generate 500mer double-stranded DNA templates. ..

    Plasmid Preparation:

    Article Title: Polymerase-amplified release of ATP (POLARA) for detecting single nucleotide variants in RNA and DNA †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03901a
    Article Snippet: .. Synthesis of RNA Targets For the JAK2 and BRAF genes, PCR was performed on plasmids2–4 containing inserts with the wild-type (JAK2: Addgene plasmid #23915) or mutant (JAK2 V617F: Addgene plasmid #64610) sequence to generate 500mer double-stranded DNA templates. ..

    Article Title: A p53/lnc‐Ip53 Negative Feedback Loop Regulates Tumor Growth and Chemoresistance
    Article Snippet: .. To examine the activity of p53 signaling, cells were transfected with 10 nM silnc-Ip53 or NC duplex for 24 hours, followed by co-transfection of 25 ng pRL-TK and 25 ng firefly luciferase reporter plasmids containing wild-type (PG13-Luc; Addgene Plasmid #16442, Cambridge, MA, USA) or mutant (MG15-Luc; Addgene Plasmid #16443) p53 binding sites upstream of the firefly luciferase gene for another 36 hours. ..

    Sequencing:

    Article Title: Polymerase-amplified release of ATP (POLARA) for detecting single nucleotide variants in RNA and DNA †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03901a
    Article Snippet: .. Synthesis of RNA Targets For the JAK2 and BRAF genes, PCR was performed on plasmids2–4 containing inserts with the wild-type (JAK2: Addgene plasmid #23915) or mutant (JAK2 V617F: Addgene plasmid #64610) sequence to generate 500mer double-stranded DNA templates. ..

    other:

    Article Title: Single-molecule characterization of target search dynamics of DNA-binding proteins in DNA-condensed droplets
    Article Snippet: For GFP, the negatively charged (−30) mutant (62936; Addgene) with a N-terminal 6 × His tag was prepared ( ).

    Article Title: Transcription factor EB (TFEB) interaction with RagC is disrupted during Enterovirus D68 Infection
    Article Snippet: The TFEB wild-type (WT-TFEB [plasmid #38119]) and mutant (Δ30-TFEB [plasmid #44445]) constructs were obtained from Addgene (deposited by Shawn Ferguson) and transfected into H1HeLa using the Lipofectamine 2000 transfection reagent.

    Article Title: Transcription factor EB (TFEB) interaction with RagC is disrupted during enterovirus D68 infection.
    Article Snippet: The Month XXXX Volume 0 Issue 0 10.1128/jvi.00556-2413 D ow nl oa de d fr om h ttp s: //j ou rn al s. as m .o rg /jo ur na l/j vi o n 05 J ul y 20 24 b y 24 05 :a cc 0: 12 07 :1 a8 1: cd 59 :6 d6 4: d6 56 :a b6 e. TFEB wild-type [WT-TFEB (plasmid #38119)] and mutant [∆30-TFEB (plasmid #44445)] constructs were obtained from Addgene (deposited by Shawn Ferguson).

    Article Title: Pericyte-Like Spreading by Disseminated Cancer Cells Activates YAP and MRTF for Metastatic Colonization
    Article Snippet: RFP was tagged at the C-terminal to a mutant (R12H/N18T/V19A/G67S) E. coli folA dihyrofolate reductase (Addgene #29236), which targets the fused protein for proteasomal degradation in the absence of its small molecule stabilizer trimethoprim (TMP) 32 .

    Activity Assay:

    Article Title: A p53/lnc‐Ip53 Negative Feedback Loop Regulates Tumor Growth and Chemoresistance
    Article Snippet: .. To examine the activity of p53 signaling, cells were transfected with 10 nM silnc-Ip53 or NC duplex for 24 hours, followed by co-transfection of 25 ng pRL-TK and 25 ng firefly luciferase reporter plasmids containing wild-type (PG13-Luc; Addgene Plasmid #16442, Cambridge, MA, USA) or mutant (MG15-Luc; Addgene Plasmid #16443) p53 binding sites upstream of the firefly luciferase gene for another 36 hours. ..

    Transfection:

    Article Title: A p53/lnc‐Ip53 Negative Feedback Loop Regulates Tumor Growth and Chemoresistance
    Article Snippet: .. To examine the activity of p53 signaling, cells were transfected with 10 nM silnc-Ip53 or NC duplex for 24 hours, followed by co-transfection of 25 ng pRL-TK and 25 ng firefly luciferase reporter plasmids containing wild-type (PG13-Luc; Addgene Plasmid #16442, Cambridge, MA, USA) or mutant (MG15-Luc; Addgene Plasmid #16443) p53 binding sites upstream of the firefly luciferase gene for another 36 hours. ..

    Luciferase:

    Article Title: A p53/lnc‐Ip53 Negative Feedback Loop Regulates Tumor Growth and Chemoresistance
    Article Snippet: .. To examine the activity of p53 signaling, cells were transfected with 10 nM silnc-Ip53 or NC duplex for 24 hours, followed by co-transfection of 25 ng pRL-TK and 25 ng firefly luciferase reporter plasmids containing wild-type (PG13-Luc; Addgene Plasmid #16442, Cambridge, MA, USA) or mutant (MG15-Luc; Addgene Plasmid #16443) p53 binding sites upstream of the firefly luciferase gene for another 36 hours. ..

    Binding Assay:

    Article Title: A p53/lnc‐Ip53 Negative Feedback Loop Regulates Tumor Growth and Chemoresistance
    Article Snippet: .. To examine the activity of p53 signaling, cells were transfected with 10 nM silnc-Ip53 or NC duplex for 24 hours, followed by co-transfection of 25 ng pRL-TK and 25 ng firefly luciferase reporter plasmids containing wild-type (PG13-Luc; Addgene Plasmid #16442, Cambridge, MA, USA) or mutant (MG15-Luc; Addgene Plasmid #16443) p53 binding sites upstream of the firefly luciferase gene for another 36 hours. ..



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    Expression of <t>FimA</t> protein and generation of mAbs targeting FimA of P. <t>gingivalis</t> . (A) SDS-PAGE analysis of purified of recombinant FimA-His (rFimA) protein. (B) Schematic of the immunisation protocol. (C) Determination of serum anti-FimA antibody titre by ELISA using rFimA-coated ELISA plates. (D) ELISA-based detection of anti-FimA mAbs in culture supernatants from five hybridoma cell lines. (E) SDS-PAGE analysis of five anti-FimA mAbs purified from mouse ascites via protein A affinity chromatography. (F) Isotype determination of anti-FimA mAbs by ELISA using HRP-conjugated antibodies specific for mouse IgM, IgG1, IgG2a, IgG2b, IgG3, IgA, κ , and λ chains.
    P Gingivalis Fima Deficient δfima Mutant, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Plasmidsaurus complement mutant strains genome sequence medium length read assemblies
    Expression of <t>FimA</t> protein and generation of mAbs targeting FimA of P. <t>gingivalis</t> . (A) SDS-PAGE analysis of purified of recombinant FimA-His (rFimA) protein. (B) Schematic of the immunisation protocol. (C) Determination of serum anti-FimA antibody titre by ELISA using rFimA-coated ELISA plates. (D) ELISA-based detection of anti-FimA mAbs in culture supernatants from five hybridoma cell lines. (E) SDS-PAGE analysis of five anti-FimA mAbs purified from mouse ascites via protein A affinity chromatography. (F) Isotype determination of anti-FimA mAbs by ELISA using HRP-conjugated antibodies specific for mouse IgM, IgG1, IgG2a, IgG2b, IgG3, IgA, κ , and λ chains.
    Complement Mutant Strains Genome Sequence Medium Length Read Assemblies, supplied by Plasmidsaurus, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Expression of <t>FimA</t> protein and generation of mAbs targeting FimA of P. <t>gingivalis</t> . (A) SDS-PAGE analysis of purified of recombinant FimA-His (rFimA) protein. (B) Schematic of the immunisation protocol. (C) Determination of serum anti-FimA antibody titre by ELISA using rFimA-coated ELISA plates. (D) ELISA-based detection of anti-FimA mAbs in culture supernatants from five hybridoma cell lines. (E) SDS-PAGE analysis of five anti-FimA mAbs purified from mouse ascites via protein A affinity chromatography. (F) Isotype determination of anti-FimA mAbs by ELISA using HRP-conjugated antibodies specific for mouse IgM, IgG1, IgG2a, IgG2b, IgG3, IgA, κ , and λ chains.
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    Image Search Results


    SIRT1 mediates the regulatory effect of NAD + on primary cilia. (a) SIRT1 activator resveratrol (20 μM) treatment elongates cilia length in N1 cells ( n = 8 wells per group). AC3: Adenylyl cyclase 3. (b) Effects of overexpression (OE) of wild–type SIRT1 and its catalytically inactive H363Y mutant on ciliary length in N1 cells ( n = 5 wells per group). (c) Effect of treatment with the SIRT1 inhibitor EX527 (100 μm for 16 h) on NR (100 μM)‐induced cilia growth ( n = 6 wells per group). (d) Sirt1 knockdown with small inhibitory RNA ( siSirt1 ) prevents NMN (100 μM)–induced cilia elongation ( n = 3 wells per group). (e) Effect of SIRT1 OE on mRNA expression levels of multiple cilia‐related genes ( n = 6 wells per group). (f) Sirt1 knockdown inhibits NMN‐induced upregulation of cilia‐related genes ( n = 6 wells per group). (g, h) SIRT1 and RFX1 cooperatively regulate the promoter activity of the Ift88 gene ( n = 3 wells per group). (i, j) Molecular interaction between SIRT1 and RFX1, and SIRT1‐mediated deacetylation of RFX1, demonstrated by sequential immunoprecipitation (IP) and immunoblotting (IB) in N1 cells with or without SIRT1 OE. Ac‐K, acetylated lysine. (k) Effect of autophagy inhibition by Atg5 knockdown or 3‐MA treatment on SIRT1‐induced changes in primary cilia ( n = 5). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t‐ test (a, e), one‐way ANOVA (b, c, f, g, h, k), or two‐way (d) ANOVA with Tukey's post hoc test. n.s., not significant. Scale bars, 20 μm.

    Journal: Aging Cell

    Article Title: A Cilia–Centered Nicotinamide Adenine Dinucleotide ( NAD + ) Signaling Network Regulates Hypothalamic Lysosomal Homeostasis and Metabolic Aging

    doi: 10.1111/acel.70745

    Figure Lengend Snippet: SIRT1 mediates the regulatory effect of NAD + on primary cilia. (a) SIRT1 activator resveratrol (20 μM) treatment elongates cilia length in N1 cells ( n = 8 wells per group). AC3: Adenylyl cyclase 3. (b) Effects of overexpression (OE) of wild–type SIRT1 and its catalytically inactive H363Y mutant on ciliary length in N1 cells ( n = 5 wells per group). (c) Effect of treatment with the SIRT1 inhibitor EX527 (100 μm for 16 h) on NR (100 μM)‐induced cilia growth ( n = 6 wells per group). (d) Sirt1 knockdown with small inhibitory RNA ( siSirt1 ) prevents NMN (100 μM)–induced cilia elongation ( n = 3 wells per group). (e) Effect of SIRT1 OE on mRNA expression levels of multiple cilia‐related genes ( n = 6 wells per group). (f) Sirt1 knockdown inhibits NMN‐induced upregulation of cilia‐related genes ( n = 6 wells per group). (g, h) SIRT1 and RFX1 cooperatively regulate the promoter activity of the Ift88 gene ( n = 3 wells per group). (i, j) Molecular interaction between SIRT1 and RFX1, and SIRT1‐mediated deacetylation of RFX1, demonstrated by sequential immunoprecipitation (IP) and immunoblotting (IB) in N1 cells with or without SIRT1 OE. Ac‐K, acetylated lysine. (k) Effect of autophagy inhibition by Atg5 knockdown or 3‐MA treatment on SIRT1‐induced changes in primary cilia ( n = 5). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t‐ test (a, e), one‐way ANOVA (b, c, f, g, h, k), or two‐way (d) ANOVA with Tukey's post hoc test. n.s., not significant. Scale bars, 20 μm.

    Article Snippet: N1 cells were transfected with wild–type SIRT1 (1 μg; Addgene, #1791), the catalytically inactive SIRT1 H363Y mutant (1 μg; Addgene, #1792), or Sirt1–targeting siRNA (100 pmol) for 48 h, or treated with the SIRT1 inhibitor EX527 (100 μM) for 16 h. Equal amounts of cell lysates were incubated with the fluorogenic acetylated substrate, NAD + , and the developer provided in the kit.

    Techniques: Over Expression, Mutagenesis, Knockdown, Expressing, Activity Assay, Immunoprecipitation, Western Blot, Inhibition

    Primary cilia are essential for NAD + ‐mediated regulation of lysosomal acidity. (a) Effects of NAD + elevation induced by NAD or its precursors (NMN, NR) treatment on lysosomal acidity, assessed by LysoSensor fluorescence intensity ( n = 6 wells per group). Scale bars, 20 μm. (b) Effect of overexpression of wild‐type SIRT1 and a catalytically inactive SIRT1 mutant ( H363Y ) on lysosomal acidity ( n = 5 wells per group). (c, d) Effects of NAD + depletion induced by FK866 treatment or Nampt knockdown on lysosomal acidity ( n = 6 wells per group). Scale bars, 20 μm. (e) Restorative effects of NMN co‐treatment on the FK866‐induced lysosomal deacidification in N1 cells transfected with control siRNA ( siControl ), Ift88 siRNA ( siIft88 ), or Ift20 siRNA ( siIft20 ) ( n = 4 wells per group). Scale bars, 20 μm. (f) Effects of NAD + depletion (FK866) and repletion (FK866 + NMN) on lysosomal cathepsin B activity, assessed by the Magic Red assay, in N1 cells with or without ciliary dysgenesis ( n = 6 wells per group). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t ‐test (c, d), one‐way ANOVA (a, b), or two‐way ANOVA (e, f), followed by Tukey's post hoc test. n.s., not significant.

    Journal: Aging Cell

    Article Title: A Cilia–Centered Nicotinamide Adenine Dinucleotide ( NAD + ) Signaling Network Regulates Hypothalamic Lysosomal Homeostasis and Metabolic Aging

    doi: 10.1111/acel.70745

    Figure Lengend Snippet: Primary cilia are essential for NAD + ‐mediated regulation of lysosomal acidity. (a) Effects of NAD + elevation induced by NAD or its precursors (NMN, NR) treatment on lysosomal acidity, assessed by LysoSensor fluorescence intensity ( n = 6 wells per group). Scale bars, 20 μm. (b) Effect of overexpression of wild‐type SIRT1 and a catalytically inactive SIRT1 mutant ( H363Y ) on lysosomal acidity ( n = 5 wells per group). (c, d) Effects of NAD + depletion induced by FK866 treatment or Nampt knockdown on lysosomal acidity ( n = 6 wells per group). Scale bars, 20 μm. (e) Restorative effects of NMN co‐treatment on the FK866‐induced lysosomal deacidification in N1 cells transfected with control siRNA ( siControl ), Ift88 siRNA ( siIft88 ), or Ift20 siRNA ( siIft20 ) ( n = 4 wells per group). Scale bars, 20 μm. (f) Effects of NAD + depletion (FK866) and repletion (FK866 + NMN) on lysosomal cathepsin B activity, assessed by the Magic Red assay, in N1 cells with or without ciliary dysgenesis ( n = 6 wells per group). Data were obtained from three independent experiments and are presented as the mean ± SEM. Statistical analyses were performed using two‐sided unpaired Student's t ‐test (c, d), one‐way ANOVA (a, b), or two‐way ANOVA (e, f), followed by Tukey's post hoc test. n.s., not significant.

    Article Snippet: N1 cells were transfected with wild–type SIRT1 (1 μg; Addgene, #1791), the catalytically inactive SIRT1 H363Y mutant (1 μg; Addgene, #1792), or Sirt1–targeting siRNA (100 pmol) for 48 h, or treated with the SIRT1 inhibitor EX527 (100 μM) for 16 h. Equal amounts of cell lysates were incubated with the fluorogenic acetylated substrate, NAD + , and the developer provided in the kit.

    Techniques: Fluorescence, Over Expression, Mutagenesis, Knockdown, Transfection, Control, Activity Assay

    Expression of FimA protein and generation of mAbs targeting FimA of P. gingivalis . (A) SDS-PAGE analysis of purified of recombinant FimA-His (rFimA) protein. (B) Schematic of the immunisation protocol. (C) Determination of serum anti-FimA antibody titre by ELISA using rFimA-coated ELISA plates. (D) ELISA-based detection of anti-FimA mAbs in culture supernatants from five hybridoma cell lines. (E) SDS-PAGE analysis of five anti-FimA mAbs purified from mouse ascites via protein A affinity chromatography. (F) Isotype determination of anti-FimA mAbs by ELISA using HRP-conjugated antibodies specific for mouse IgM, IgG1, IgG2a, IgG2b, IgG3, IgA, κ , and λ chains.

    Journal: Journal of Oral Microbiology

    Article Title: Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis

    doi: 10.1080/20002297.2026.2729552

    Figure Lengend Snippet: Expression of FimA protein and generation of mAbs targeting FimA of P. gingivalis . (A) SDS-PAGE analysis of purified of recombinant FimA-His (rFimA) protein. (B) Schematic of the immunisation protocol. (C) Determination of serum anti-FimA antibody titre by ELISA using rFimA-coated ELISA plates. (D) ELISA-based detection of anti-FimA mAbs in culture supernatants from five hybridoma cell lines. (E) SDS-PAGE analysis of five anti-FimA mAbs purified from mouse ascites via protein A affinity chromatography. (F) Isotype determination of anti-FimA mAbs by ELISA using HRP-conjugated antibodies specific for mouse IgM, IgG1, IgG2a, IgG2b, IgG3, IgA, κ , and λ chains.

    Article Snippet: The P. gingivalis FimA-deficient (ΔfimA) mutant in the ATCC 33277 background was constructed as previously described with minor modifications [ ].

    Techniques: Expressing, SDS Page, Analysis, Purification, Recombinant, Enzyme-linked Immunosorbent Assay, Affinity Chromatography

    Binding analysis of anti-FimA mAbs to FimA. (A) Binding kinetics of anti-FimA mAbs to rFimA protein determined by biolayer interferometry (BLI). Sensorgrams show a dilution series of antibodies (200 to 12.5 nM), with data fitted globally using a 1:1 binding model. (B) Representative ELISA binding curves of the mAbs to immobilised rFimA protein. Bound antibodies were detected with HRP-conjugated anti-mouse IgG secondary antibody and reported as absorbance at 450 nm. (C) Summary of binding affinity (KD), association rate (ka), dissociation rate (kdis), and half-maximal effective concentration (EC50) values for each mAb. (D) Representative immunofluorescence images of mAb binding to P. gingivalis cells FimA fimbriae. Bacterial DNA was stained with Hoechst (blue). Cells were incubated with control IgG or anti-FimA mAbs, followed by Alexa Fluor 546-conjugated anti-mouse IgG antibody (red). Merged images are shown in the bottom panel. Scale bar, 2 μm.

    Journal: Journal of Oral Microbiology

    Article Title: Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis

    doi: 10.1080/20002297.2026.2729552

    Figure Lengend Snippet: Binding analysis of anti-FimA mAbs to FimA. (A) Binding kinetics of anti-FimA mAbs to rFimA protein determined by biolayer interferometry (BLI). Sensorgrams show a dilution series of antibodies (200 to 12.5 nM), with data fitted globally using a 1:1 binding model. (B) Representative ELISA binding curves of the mAbs to immobilised rFimA protein. Bound antibodies were detected with HRP-conjugated anti-mouse IgG secondary antibody and reported as absorbance at 450 nm. (C) Summary of binding affinity (KD), association rate (ka), dissociation rate (kdis), and half-maximal effective concentration (EC50) values for each mAb. (D) Representative immunofluorescence images of mAb binding to P. gingivalis cells FimA fimbriae. Bacterial DNA was stained with Hoechst (blue). Cells were incubated with control IgG or anti-FimA mAbs, followed by Alexa Fluor 546-conjugated anti-mouse IgG antibody (red). Merged images are shown in the bottom panel. Scale bar, 2 μm.

    Article Snippet: The P. gingivalis FimA-deficient (ΔfimA) mutant in the ATCC 33277 background was constructed as previously described with minor modifications [ ].

    Techniques: Binding Assay, Analysis, Enzyme-linked Immunosorbent Assay, Association Rate Constant, Dissociation Rate Constant, Concentration Assay, Immunofluorescence, Staining, Incubation, Control

    Specificity and epitope diversity of anti‑FimA mAbs. (A) Western blot analysis of anti-FimA mAbs using whole-cell lysates of P. gingivalis and other bacteria; rFimA protein was included as a positive control. (B) Cross-reactivity of anti-FimA mAbs assessed by ELISA. (C-D) Flow cytometry analysis of mAbs binding to P. gingivalis ATCC33277 (C) and other bacteria (D) compared with PBS (red) and isotype IgG (black) controls. Median fluorescence intensity (MFI) was determined from three independent experiments (mean ± SD; one‑way ANOVA with Dunnett’s test, ***p < 0.001). (E) Epitope binning by BLI competition assay. (F) Summary of BLI-based competitive binding results among the five anti-FimA mAbs.

    Journal: Journal of Oral Microbiology

    Article Title: Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis

    doi: 10.1080/20002297.2026.2729552

    Figure Lengend Snippet: Specificity and epitope diversity of anti‑FimA mAbs. (A) Western blot analysis of anti-FimA mAbs using whole-cell lysates of P. gingivalis and other bacteria; rFimA protein was included as a positive control. (B) Cross-reactivity of anti-FimA mAbs assessed by ELISA. (C-D) Flow cytometry analysis of mAbs binding to P. gingivalis ATCC33277 (C) and other bacteria (D) compared with PBS (red) and isotype IgG (black) controls. Median fluorescence intensity (MFI) was determined from three independent experiments (mean ± SD; one‑way ANOVA with Dunnett’s test, ***p < 0.001). (E) Epitope binning by BLI competition assay. (F) Summary of BLI-based competitive binding results among the five anti-FimA mAbs.

    Article Snippet: The P. gingivalis FimA-deficient (ΔfimA) mutant in the ATCC 33277 background was constructed as previously described with minor modifications [ ].

    Techniques: Western Blot, Analysis, Bacteria, Positive Control, Enzyme-linked Immunosorbent Assay, Flow Cytometry, Binding Assay, Fluorescence, Epitope Binning, Competitive Binding Assay

    Anti-FimA mAbs inhibit P. gingivalis adhesion. (A) SEM images of P. gingivalis adhesion to sHA beads following treatment with control IgG or anti-FimA mAbs. Scale bar, 5 µm. (B) qPCR quantification of bound P. gingivalis 16S rRNA gene copies on sHA beads. (C) Fluorescence microscopy images of DilC18(3)-labelled P. gingivalis (red) binding to SYTO9 stained S. gordonii biofilms (green) following pre-treatment with control IgG or anti-FimA mAbs. Scale bar, 200 µm. (D) Quantification of adhesion was performed in ImageJ based on the area of red fluorescence (Dil) from P. gingivalis colocalized with the green biofilm. Data are presented as mean ± SD and were analysed by one‑way ANOVA with Dunnett’s test, ***p < 0.001.

    Journal: Journal of Oral Microbiology

    Article Title: Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis

    doi: 10.1080/20002297.2026.2729552

    Figure Lengend Snippet: Anti-FimA mAbs inhibit P. gingivalis adhesion. (A) SEM images of P. gingivalis adhesion to sHA beads following treatment with control IgG or anti-FimA mAbs. Scale bar, 5 µm. (B) qPCR quantification of bound P. gingivalis 16S rRNA gene copies on sHA beads. (C) Fluorescence microscopy images of DilC18(3)-labelled P. gingivalis (red) binding to SYTO9 stained S. gordonii biofilms (green) following pre-treatment with control IgG or anti-FimA mAbs. Scale bar, 200 µm. (D) Quantification of adhesion was performed in ImageJ based on the area of red fluorescence (Dil) from P. gingivalis colocalized with the green biofilm. Data are presented as mean ± SD and were analysed by one‑way ANOVA with Dunnett’s test, ***p < 0.001.

    Article Snippet: The P. gingivalis FimA-deficient (ΔfimA) mutant in the ATCC 33277 background was constructed as previously described with minor modifications [ ].

    Techniques: Control, Fluorescence, Microscopy, Binding Assay, Staining

    Functional assessment of anti‑FimA mAbs in complement‑mediated killing and phagocytosis of P. gingivalis . (A−B) Complement‑mediated killing assay. P. gingivalis was incubated with guinea pig complement serum in the presence of anti‑FimA mAbs, isotype control IgG (100 µg/mL), or without antibody (Mock). (A) Bacterial suspensions were stained with a LIVE/DEAD viability kit; the percentage of live versus dead cells was quantified based on fluorescent signal using ImageJ software. (B) Bacterial survival was determined by colony-forming unit (CFU) counts and expressed as a percentage of the IgG control. (C-G) Macrophage phagocytosis assay. FITC‑labelled P. gingivalis was pre‑treated with anti‑FimA mAbs or IgG control and then co‑cultured with macrophages at an MOI of 100. (C) Representative fluorescence microscopy images showing macrophages (F-actin, red; nuclei, blue) with ingested bacteria (green). Scale bar, 200 µm. (D) Quantitative analysis based on fluorescent signal area using ImageJ software. (E) Flow cytometry analysis of FITC fluorescence in macrophages, showing the percentage of FITC-positive cells. (F) Percentage of macrophages with internalised bacteria. (G) Phagocytic Index defined as (percentage of macrophages with internalised bacteria) × (mean fluorescence intensity, MFI)/100. All data are presented as mean ± SD from at least three independent experiments and were analysed by one‑way ANOVA with Dunnett’s test ( *p < 0.05, **p < 0.01, ***p < 0.001; ns, not significant).

    Journal: Journal of Oral Microbiology

    Article Title: Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis

    doi: 10.1080/20002297.2026.2729552

    Figure Lengend Snippet: Functional assessment of anti‑FimA mAbs in complement‑mediated killing and phagocytosis of P. gingivalis . (A−B) Complement‑mediated killing assay. P. gingivalis was incubated with guinea pig complement serum in the presence of anti‑FimA mAbs, isotype control IgG (100 µg/mL), or without antibody (Mock). (A) Bacterial suspensions were stained with a LIVE/DEAD viability kit; the percentage of live versus dead cells was quantified based on fluorescent signal using ImageJ software. (B) Bacterial survival was determined by colony-forming unit (CFU) counts and expressed as a percentage of the IgG control. (C-G) Macrophage phagocytosis assay. FITC‑labelled P. gingivalis was pre‑treated with anti‑FimA mAbs or IgG control and then co‑cultured with macrophages at an MOI of 100. (C) Representative fluorescence microscopy images showing macrophages (F-actin, red; nuclei, blue) with ingested bacteria (green). Scale bar, 200 µm. (D) Quantitative analysis based on fluorescent signal area using ImageJ software. (E) Flow cytometry analysis of FITC fluorescence in macrophages, showing the percentage of FITC-positive cells. (F) Percentage of macrophages with internalised bacteria. (G) Phagocytic Index defined as (percentage of macrophages with internalised bacteria) × (mean fluorescence intensity, MFI)/100. All data are presented as mean ± SD from at least three independent experiments and were analysed by one‑way ANOVA with Dunnett’s test ( *p < 0.05, **p < 0.01, ***p < 0.001; ns, not significant).

    Article Snippet: The P. gingivalis FimA-deficient (ΔfimA) mutant in the ATCC 33277 background was constructed as previously described with minor modifications [ ].

    Techniques: Functional Assay, Incubation, Control, Staining, Software, Phagocytosis Assay, Fluorescence, Microscopy, Bacteria, Analysis, Flow Cytometry

    Anti‑FimA mAbs induce auto-aggregation and modulate biofilm formation in P. gingivalis . (A) Auto‑aggregation of P. gingivalis induced by anti‑FimA mAbs. Bacteria were treated with the indicated mAbs or isotype control IgG (100 µg/mL) for 2 h at room temperature. Representative images show Gram‑stained bacterial aggregates visualised by light microscopy (Top) and macroscopic appearance (Bottom). (B) Aggregation kinetics monitored by the decrease in OD600 of the culture supernatant over 120 min. Data are normalised to the initial OD600 value (set as 100%). (C) Representative images of crystal violet‑stained biofilms formed in the presence of control IgG or anti‑FimA mAbs. (D) Biofilm biomass was quantified by absorbance at 600 nm. (F) SEM micrographs showing P. gingivalis biofilms formed after 48 h of exposure to control IgG or different anti‑FimA mAbs. All data are mean ± SD from three independent experiments and were analysed by one-way ANOVA analysis with Dunnett’s test ( * * * p < 0.001).

    Journal: Journal of Oral Microbiology

    Article Title: Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis

    doi: 10.1080/20002297.2026.2729552

    Figure Lengend Snippet: Anti‑FimA mAbs induce auto-aggregation and modulate biofilm formation in P. gingivalis . (A) Auto‑aggregation of P. gingivalis induced by anti‑FimA mAbs. Bacteria were treated with the indicated mAbs or isotype control IgG (100 µg/mL) for 2 h at room temperature. Representative images show Gram‑stained bacterial aggregates visualised by light microscopy (Top) and macroscopic appearance (Bottom). (B) Aggregation kinetics monitored by the decrease in OD600 of the culture supernatant over 120 min. Data are normalised to the initial OD600 value (set as 100%). (C) Representative images of crystal violet‑stained biofilms formed in the presence of control IgG or anti‑FimA mAbs. (D) Biofilm biomass was quantified by absorbance at 600 nm. (F) SEM micrographs showing P. gingivalis biofilms formed after 48 h of exposure to control IgG or different anti‑FimA mAbs. All data are mean ± SD from three independent experiments and were analysed by one-way ANOVA analysis with Dunnett’s test ( * * * p < 0.001).

    Article Snippet: The P. gingivalis FimA-deficient (ΔfimA) mutant in the ATCC 33277 background was constructed as previously described with minor modifications [ ].

    Techniques: Bacteria, Control, Light Microscopy, Analysis