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6xhis Brd4 Bd1 Bd2, supplied by BPS Bioscience, 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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bd2 domains  (BPS Bioscience)
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Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 <t>BD1-BD2</t> (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .
Bd2 Domains, supplied by BPS Bioscience, 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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brd4 bd1 bd2 bps bioscience  (BPS Bioscience)
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BPS Bioscience brd4 bd1 bd2 bps bioscience
Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 <t>BD1-BD2</t> (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .
Brd4 Bd1 Bd2 Bps Bioscience, supplied by BPS Bioscience, 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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brd4  (BPS Bioscience)
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BPS Bioscience brd4
Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 <t>BD1-BD2</t> (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .
Brd4, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human brd4  (BPS Bioscience)
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Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 <t>BD1-BD2</t> (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .
Human Brd4, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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brd4 bd1 bd2 gst tag  (BPS Bioscience)
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Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 <t>BD1-BD2</t> (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .
Brd4 Bd1 Bd2 Gst Tag, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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brd4 (bd1+bd2) tr-fret assay kit  (BPS Bioscience)
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BPS Bioscience brd4 (bd1+bd2) tr-fret assay kit
Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 <t>BD1-BD2</t> (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .
Brd4 (Bd1+Bd2) Tr Fret Assay Kit, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 BD1-BD2 (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .

Journal: Cell Reports Medicine

Article Title: A triple-action PROTAC for wild-type p53 cancer therapy

doi: 10.1016/j.xcrm.2025.102467

Figure Lengend Snippet: Design and in vitro activity of TAPTAC1 (A) A chimera composed of a stapled p53 peptide and a small molecule BET protein inhibitor was designed to achieve triple-action targeting of HDM2, HDMX, and BET proteins to maximally restore p53 while hijacking HDM2 to degrade an oncogenic driver (BET proteins) instead of a tumor suppressor (p53). (B) Chemical composition of TAPTAC1, which links the BET inhibitor JQ1 to the stapled p53 peptide via a lysine-βAla moiety installed at position 25 of the p53 transactivation helix. (C) MD simulations demonstrate the assembly of a ternary complex between TAPTAC1 and the respective JQ1- and p53-binding domains of BRD4 and HDM2. (D) TAPTAC1 effectively generated ternary complexes (green) between the BD1 domain of BRD4 and HDM2 (left) and HDMX (right). Control elution profiles are shown for the individual proteins alone, including BRD4 BD1 (cyan), HDM2 (red), and HDMX (orange), and their combinations, including BRD4 BD1 and HDM2 (purple) and BRD4 BD1 and HDMX (brown). Each SEC experiment was repeated twice using independent preparations of proteins with similar results. (E) An in vitro ubiquitylation assay demonstrated the natural selectivity of HDM2 for p53, as evidenced by time-dependent laddering of p53 but not BRD4 BD1-BD2 (left 4 lanes). In the presence of TAPTAC1, the primary target of HDM2 is switched from p53 to BRD4 BD1-BD2 , which exhibits newfound laddering at the expense of p53 (right 4 lanes). Ubiquitylation assays were repeated three times with independent preparations of proteins and reagents with similar results. See also and .

Article Snippet: Recombinant FLAG-p53 (20 μM, BPS Bioscience, 100412) and recombinant 6xHis-BRD4 bearing BD1 and BD2 domains (20 μM, BPS Bioscience, 31045) were added as substrates for the ubiquitylation assay, in the absence or presence of TAPTAC1 (60 μM), and incubated for 0, 1, 2, or 4 h. Reactions were stopped with LDS buffer (Invitrogen) and boiled at 95°C for 5 min.

Techniques: In Vitro, Activity Assay, Binding Assay, Generated, Control, Ubiquitin Assay