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  • 95
    Chem Impex International γ benzyl l
    γ Benzyl L, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    MedChemExpress opaganib
    Opaganib, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech mms19
    a Domain organisation of human DNA2, with the four FeS cluster-coordinating cysteines highlighted. b Radioactive iron-55 incorporation in wild-type DNA2 and cysteine variants, measured by liquid scintillation counting. Data are expressed relative to wild-type, which is set to 100% ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). c Iron incorporation as in b for wild-type, nuclease-deficient (D277A) and helicase-deficient (K654R) DNA2, with or without FeS cluster-deficiency (C396S) ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). d FLAG-DNA2 WT, C136S and C396S over-expressed in HEK293T cells were immunoprecipitated, and co-immunoprecipitation with endogenous <t>MMS19,</t> CIAO1 and MIP18 was assessed by SDS–PAGE and Western blotting. e Stability of inducibly expressed FLAG-DNA2 WT and FLAG-DNA2 C396S over time upon addition of cycloheximide (CHX), analysed by SDS–PAGE and Western blotting.
    Mms19, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Addgene inc plasmids pcdna3 1 v5 his snk hplk227
    a Domain organisation of human DNA2, with the four FeS cluster-coordinating cysteines highlighted. b Radioactive iron-55 incorporation in wild-type DNA2 and cysteine variants, measured by liquid scintillation counting. Data are expressed relative to wild-type, which is set to 100% ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). c Iron incorporation as in b for wild-type, nuclease-deficient (D277A) and helicase-deficient (K654R) DNA2, with or without FeS cluster-deficiency (C396S) ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). d FLAG-DNA2 WT, C136S and C396S over-expressed in HEK293T cells were immunoprecipitated, and co-immunoprecipitation with endogenous <t>MMS19,</t> CIAO1 and MIP18 was assessed by SDS–PAGE and Western blotting. e Stability of inducibly expressed FLAG-DNA2 WT and FLAG-DNA2 C396S over time upon addition of cycloheximide (CHX), analysed by SDS–PAGE and Western blotting.
    Plasmids Pcdna3 1 V5 His Snk Hplk227, supplied by Addgene inc, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech rabbit anti mms19
    Cdkal1 protein interacts with the cytosolic iron–sulfur cluster transfer complex proteins and the adenine nucleotide transporter ANT1 . (A) Proteins interacting with CDKAL1 as identified in this study by co-immunoprecipitation of FLAG-CDKAL1 followed by mass spectrometry (purple arrows). CDKAL1 protein interactors include components of the cytosolic Fe-S cluster transfer complex <t>(MMS19,</t> FAM96B, and CIAO1) and the mitochondrial protein ANT1. Reciprocal interaction of ANT1 with endogenous CDKAL1 is also represented. Also shown is the interaction of MMS19 with endogenous CDKAL1 from the BioPlex interactome project (black arrow) . (B) Co-immunoprecipitation of endogenous CDKAL1 with FLAG-tagged ANT1. (C) Diagram of FLAG-tagged CDKAL1 mutants used in this study. Input (D) and (E) co-immunoprecipitation of FLAG-tagged wild type CDKAL1 or CDKAL1 mutants. Shown are immunoblots for FLAG-CDKAL1, MMS19, FAM96B, and ANT1 following anti-FLAG immunoprecipitation from lysates of HEK293 cells transfected with empty pcDNA 3.1 vector (Ctrl) or pcDNA 3.1 expressing: wild-type full-length CDKAL1 (WT); full-length CDKAL1 with radical SAM domain catalytic-site cysteines mutated to alanine (AAA); truncation mutants that include only (N) or lack (ΔN) an N-terminal fragment containing the UPF004 N-terminal MTT domain; and truncations mutants that comprise only (C) or lack (ΔC) a C-terminal fragment containing the TRAM domain. Protein levels of ANT1, CDKAL1 and β-tubulin in chow-fed control or A-KO eWAT (F) or iWAT (G).
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    Image Search Results


    a Domain organisation of human DNA2, with the four FeS cluster-coordinating cysteines highlighted. b Radioactive iron-55 incorporation in wild-type DNA2 and cysteine variants, measured by liquid scintillation counting. Data are expressed relative to wild-type, which is set to 100% ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). c Iron incorporation as in b for wild-type, nuclease-deficient (D277A) and helicase-deficient (K654R) DNA2, with or without FeS cluster-deficiency (C396S) ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). d FLAG-DNA2 WT, C136S and C396S over-expressed in HEK293T cells were immunoprecipitated, and co-immunoprecipitation with endogenous MMS19, CIAO1 and MIP18 was assessed by SDS–PAGE and Western blotting. e Stability of inducibly expressed FLAG-DNA2 WT and FLAG-DNA2 C396S over time upon addition of cycloheximide (CHX), analysed by SDS–PAGE and Western blotting.

    Journal: Communications Biology

    Article Title: The iron–sulphur cluster in human DNA2 is required for all biochemical activities of DNA2

    doi: 10.1038/s42003-020-1048-4

    Figure Lengend Snippet: a Domain organisation of human DNA2, with the four FeS cluster-coordinating cysteines highlighted. b Radioactive iron-55 incorporation in wild-type DNA2 and cysteine variants, measured by liquid scintillation counting. Data are expressed relative to wild-type, which is set to 100% ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). c Iron incorporation as in b for wild-type, nuclease-deficient (D277A) and helicase-deficient (K654R) DNA2, with or without FeS cluster-deficiency (C396S) ( n = 3 independent experiments; error bars, SD). Statistical analysis: ordinary one-way ANOVA (**** p < 0.0001). d FLAG-DNA2 WT, C136S and C396S over-expressed in HEK293T cells were immunoprecipitated, and co-immunoprecipitation with endogenous MMS19, CIAO1 and MIP18 was assessed by SDS–PAGE and Western blotting. e Stability of inducibly expressed FLAG-DNA2 WT and FLAG-DNA2 C396S over time upon addition of cycloheximide (CHX), analysed by SDS–PAGE and Western blotting.

    Article Snippet: The following primary antibodies (at a dilution of 1:1000) were used: β-actin-horseradish peroxidase (HRP) (C4, sc-47778; Santa Cruz Biotechnology), DNA2 (ab96488; Abcam), CIAO1 (ab83088; Abcam), MIP18/FAM96b (20108-1-AP; Proteintech), MMS19 (16015-1-AP; Proteintech).

    Techniques: Immunoprecipitation, SDS Page, Western Blot

    Cdkal1 protein interacts with the cytosolic iron–sulfur cluster transfer complex proteins and the adenine nucleotide transporter ANT1 . (A) Proteins interacting with CDKAL1 as identified in this study by co-immunoprecipitation of FLAG-CDKAL1 followed by mass spectrometry (purple arrows). CDKAL1 protein interactors include components of the cytosolic Fe-S cluster transfer complex (MMS19, FAM96B, and CIAO1) and the mitochondrial protein ANT1. Reciprocal interaction of ANT1 with endogenous CDKAL1 is also represented. Also shown is the interaction of MMS19 with endogenous CDKAL1 from the BioPlex interactome project (black arrow) . (B) Co-immunoprecipitation of endogenous CDKAL1 with FLAG-tagged ANT1. (C) Diagram of FLAG-tagged CDKAL1 mutants used in this study. Input (D) and (E) co-immunoprecipitation of FLAG-tagged wild type CDKAL1 or CDKAL1 mutants. Shown are immunoblots for FLAG-CDKAL1, MMS19, FAM96B, and ANT1 following anti-FLAG immunoprecipitation from lysates of HEK293 cells transfected with empty pcDNA 3.1 vector (Ctrl) or pcDNA 3.1 expressing: wild-type full-length CDKAL1 (WT); full-length CDKAL1 with radical SAM domain catalytic-site cysteines mutated to alanine (AAA); truncation mutants that include only (N) or lack (ΔN) an N-terminal fragment containing the UPF004 N-terminal MTT domain; and truncations mutants that comprise only (C) or lack (ΔC) a C-terminal fragment containing the TRAM domain. Protein levels of ANT1, CDKAL1 and β-tubulin in chow-fed control or A-KO eWAT (F) or iWAT (G).

    Journal: Molecular Metabolism

    Article Title: Cdkal1, a type 2 diabetes susceptibility gene, regulates mitochondrial function in adipose tissue

    doi: 10.1016/j.molmet.2017.07.013

    Figure Lengend Snippet: Cdkal1 protein interacts with the cytosolic iron–sulfur cluster transfer complex proteins and the adenine nucleotide transporter ANT1 . (A) Proteins interacting with CDKAL1 as identified in this study by co-immunoprecipitation of FLAG-CDKAL1 followed by mass spectrometry (purple arrows). CDKAL1 protein interactors include components of the cytosolic Fe-S cluster transfer complex (MMS19, FAM96B, and CIAO1) and the mitochondrial protein ANT1. Reciprocal interaction of ANT1 with endogenous CDKAL1 is also represented. Also shown is the interaction of MMS19 with endogenous CDKAL1 from the BioPlex interactome project (black arrow) . (B) Co-immunoprecipitation of endogenous CDKAL1 with FLAG-tagged ANT1. (C) Diagram of FLAG-tagged CDKAL1 mutants used in this study. Input (D) and (E) co-immunoprecipitation of FLAG-tagged wild type CDKAL1 or CDKAL1 mutants. Shown are immunoblots for FLAG-CDKAL1, MMS19, FAM96B, and ANT1 following anti-FLAG immunoprecipitation from lysates of HEK293 cells transfected with empty pcDNA 3.1 vector (Ctrl) or pcDNA 3.1 expressing: wild-type full-length CDKAL1 (WT); full-length CDKAL1 with radical SAM domain catalytic-site cysteines mutated to alanine (AAA); truncation mutants that include only (N) or lack (ΔN) an N-terminal fragment containing the UPF004 N-terminal MTT domain; and truncations mutants that comprise only (C) or lack (ΔC) a C-terminal fragment containing the TRAM domain. Protein levels of ANT1, CDKAL1 and β-tubulin in chow-fed control or A-KO eWAT (F) or iWAT (G).

    Article Snippet: Primary antibodies used in this study include: rabbit anti-Cdkal1 (abcam, ab68045), mouse anti-ANT1 (abcam, 110322), rabbit anti-MMS19 (Proteintech, 16015-1-AP), mouse anti-total OXPHOS rodent cocktail (abcam, ab110413), mouse anti-FAM96B (Santa Cruz, sc-376801), mouse anti-FLAG tag (Sigma, F1804), mouse anti-FLAG M2 HRP-conjugated (Sigma, A8592), rabbit anti-UCP1 (abcam, 23841), and rabbit anti-β-Tubulin (Cell Signaling, 2146).

    Techniques: Immunoprecipitation, Mass Spectrometry, Western Blot, Transfection, Plasmid Preparation, Expressing