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human p300 cdna fragments  (Addgene inc)


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    Addgene inc human p300 cdna fragments
    Design and characterization of engineered mitochondrial acetyltransferase; eMAT (A) Schematic structure of eMAT. Mitochondria targeting sequence (MTS) of PDHA1, COX4, NDUFS1, SIRT4, and CAMP were fused with <t>p300</t> HAT domain (1282–1667 a.a.) or Core domain (965–1810 a.a.). (B) Subcellular localization of the fusion constructs (anti-FLAG, colored in green). PDHA1-HAT and COX4-HAT merged with a mitochondria marker protein ETFβ (colored in red). The blue signal indicates DAPI (nuclear marker). Box with magenta; constructs that showed mitochondrial localization. Scale bar: 10 μm. (C) Immunoblot images of total cell lysates from HEK293T transfected with indicated constructs. Top; anti-AcK antibody, Middle; anti-FLAG antibody, Bottom; anti-α-tubulin antibody as a loading control. (D) Immunoblot analysis of protein acetylation in mitochondria. Mitochondria were isolated from HEK293T cells transfected with indicated constructs, and immunoblot analysis was performed with anti-AcK (top), anti-FLAG (middle), and anti-ETFβ as mitochondria loading control (bottom). (E) Structure of eMAT. Top; schematic amino acid sequence of eMAT. Bottom; Structure of eMAT protein predicted with AlphaFold2 based ColabFold program (v1.5.3).
    Human P300 Cdna Fragments, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+p300+cdna+fragments/pmc12357098-383-6-13?v=Addgene+inc
    Average 93 stars, based on 30 article reviews
    human p300 cdna fragments - by Bioz Stars, 2026-07
    93/100 stars

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    1) Product Images from "Mitochondrial hyper-acetylation induced by an engineered acetyltransferase promotes cellular senescence"

    Article Title: Mitochondrial hyper-acetylation induced by an engineered acetyltransferase promotes cellular senescence

    Journal: iScience

    doi: 10.1016/j.isci.2025.113233

    Design and characterization of engineered mitochondrial acetyltransferase; eMAT (A) Schematic structure of eMAT. Mitochondria targeting sequence (MTS) of PDHA1, COX4, NDUFS1, SIRT4, and CAMP were fused with p300 HAT domain (1282–1667 a.a.) or Core domain (965–1810 a.a.). (B) Subcellular localization of the fusion constructs (anti-FLAG, colored in green). PDHA1-HAT and COX4-HAT merged with a mitochondria marker protein ETFβ (colored in red). The blue signal indicates DAPI (nuclear marker). Box with magenta; constructs that showed mitochondrial localization. Scale bar: 10 μm. (C) Immunoblot images of total cell lysates from HEK293T transfected with indicated constructs. Top; anti-AcK antibody, Middle; anti-FLAG antibody, Bottom; anti-α-tubulin antibody as a loading control. (D) Immunoblot analysis of protein acetylation in mitochondria. Mitochondria were isolated from HEK293T cells transfected with indicated constructs, and immunoblot analysis was performed with anti-AcK (top), anti-FLAG (middle), and anti-ETFβ as mitochondria loading control (bottom). (E) Structure of eMAT. Top; schematic amino acid sequence of eMAT. Bottom; Structure of eMAT protein predicted with AlphaFold2 based ColabFold program (v1.5.3).
    Figure Legend Snippet: Design and characterization of engineered mitochondrial acetyltransferase; eMAT (A) Schematic structure of eMAT. Mitochondria targeting sequence (MTS) of PDHA1, COX4, NDUFS1, SIRT4, and CAMP were fused with p300 HAT domain (1282–1667 a.a.) or Core domain (965–1810 a.a.). (B) Subcellular localization of the fusion constructs (anti-FLAG, colored in green). PDHA1-HAT and COX4-HAT merged with a mitochondria marker protein ETFβ (colored in red). The blue signal indicates DAPI (nuclear marker). Box with magenta; constructs that showed mitochondrial localization. Scale bar: 10 μm. (C) Immunoblot images of total cell lysates from HEK293T transfected with indicated constructs. Top; anti-AcK antibody, Middle; anti-FLAG antibody, Bottom; anti-α-tubulin antibody as a loading control. (D) Immunoblot analysis of protein acetylation in mitochondria. Mitochondria were isolated from HEK293T cells transfected with indicated constructs, and immunoblot analysis was performed with anti-AcK (top), anti-FLAG (middle), and anti-ETFβ as mitochondria loading control (bottom). (E) Structure of eMAT. Top; schematic amino acid sequence of eMAT. Bottom; Structure of eMAT protein predicted with AlphaFold2 based ColabFold program (v1.5.3).

    Techniques Used: Sequencing, Construct, Marker, Western Blot, Transfection, Control, Isolation



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    human p300 cdna fragments  (Addgene inc)
    93
    Addgene inc human p300 cdna fragments
    Design and characterization of engineered mitochondrial acetyltransferase; eMAT (A) Schematic structure of eMAT. Mitochondria targeting sequence (MTS) of PDHA1, COX4, NDUFS1, SIRT4, and CAMP were fused with <t>p300</t> HAT domain (1282–1667 a.a.) or Core domain (965–1810 a.a.). (B) Subcellular localization of the fusion constructs (anti-FLAG, colored in green). PDHA1-HAT and COX4-HAT merged with a mitochondria marker protein ETFβ (colored in red). The blue signal indicates DAPI (nuclear marker). Box with magenta; constructs that showed mitochondrial localization. Scale bar: 10 μm. (C) Immunoblot images of total cell lysates from HEK293T transfected with indicated constructs. Top; anti-AcK antibody, Middle; anti-FLAG antibody, Bottom; anti-α-tubulin antibody as a loading control. (D) Immunoblot analysis of protein acetylation in mitochondria. Mitochondria were isolated from HEK293T cells transfected with indicated constructs, and immunoblot analysis was performed with anti-AcK (top), anti-FLAG (middle), and anti-ETFβ as mitochondria loading control (bottom). (E) Structure of eMAT. Top; schematic amino acid sequence of eMAT. Bottom; Structure of eMAT protein predicted with AlphaFold2 based ColabFold program (v1.5.3).
    Human P300 Cdna Fragments, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+p300+cdna+fragments/pmc12357098-383-6-13?v=Addgene+inc
    Average 93 stars, based on 1 article reviews
    human p300 cdna fragments - by Bioz Stars, 2026-07
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Design and characterization of engineered mitochondrial acetyltransferase; eMAT (A) Schematic structure of eMAT. Mitochondria targeting sequence (MTS) of PDHA1, COX4, NDUFS1, SIRT4, and CAMP were fused with p300 HAT domain (1282–1667 a.a.) or Core domain (965–1810 a.a.). (B) Subcellular localization of the fusion constructs (anti-FLAG, colored in green). PDHA1-HAT and COX4-HAT merged with a mitochondria marker protein ETFβ (colored in red). The blue signal indicates DAPI (nuclear marker). Box with magenta; constructs that showed mitochondrial localization. Scale bar: 10 μm. (C) Immunoblot images of total cell lysates from HEK293T transfected with indicated constructs. Top; anti-AcK antibody, Middle; anti-FLAG antibody, Bottom; anti-α-tubulin antibody as a loading control. (D) Immunoblot analysis of protein acetylation in mitochondria. Mitochondria were isolated from HEK293T cells transfected with indicated constructs, and immunoblot analysis was performed with anti-AcK (top), anti-FLAG (middle), and anti-ETFβ as mitochondria loading control (bottom). (E) Structure of eMAT. Top; schematic amino acid sequence of eMAT. Bottom; Structure of eMAT protein predicted with AlphaFold2 based ColabFold program (v1.5.3).

    Journal: iScience

    Article Title: Mitochondrial hyper-acetylation induced by an engineered acetyltransferase promotes cellular senescence

    doi: 10.1016/j.isci.2025.113233

    Figure Lengend Snippet: Design and characterization of engineered mitochondrial acetyltransferase; eMAT (A) Schematic structure of eMAT. Mitochondria targeting sequence (MTS) of PDHA1, COX4, NDUFS1, SIRT4, and CAMP were fused with p300 HAT domain (1282–1667 a.a.) or Core domain (965–1810 a.a.). (B) Subcellular localization of the fusion constructs (anti-FLAG, colored in green). PDHA1-HAT and COX4-HAT merged with a mitochondria marker protein ETFβ (colored in red). The blue signal indicates DAPI (nuclear marker). Box with magenta; constructs that showed mitochondrial localization. Scale bar: 10 μm. (C) Immunoblot images of total cell lysates from HEK293T transfected with indicated constructs. Top; anti-AcK antibody, Middle; anti-FLAG antibody, Bottom; anti-α-tubulin antibody as a loading control. (D) Immunoblot analysis of protein acetylation in mitochondria. Mitochondria were isolated from HEK293T cells transfected with indicated constructs, and immunoblot analysis was performed with anti-AcK (top), anti-FLAG (middle), and anti-ETFβ as mitochondria loading control (bottom). (E) Structure of eMAT. Top; schematic amino acid sequence of eMAT. Bottom; Structure of eMAT protein predicted with AlphaFold2 based ColabFold program (v1.5.3).

    Article Snippet: Plasmids for eMAT were constructed from human p300 cDNA fragments amplified from pCMVβ-p300-myc (addgene#30489), or pCMVβ-p300.DY-myc (addgene#30490) for the catalytic mutant.

    Techniques: Sequencing, Construct, Marker, Western Blot, Transfection, Control, Isolation