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halotag® fusion proteins  (Promega)

 
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    Promega halotag® fusion proteins
    In-cell binding analysis between ETO2 and the GATAD2A (M) PPPL region. ( A ) A diagram depicts the different <t>NanoLuc</t> (NL) <t>and</t> <t>HaloTag</t> (HT) constructs for binding analysis by bioluminescence resonance energy transfer (NanoBRET). Six different ( M )PPPL constructs were designed, including two with the NL donor tag on the C -termini (one including the neighboring CR1 domain as a coiled-coil single chain sequence on the N -terminus, see Materials and methods). The remaining four ( M )PPPL constructs contain the NL tag on the N -terminus to allow for C -terminal truncation while maintaining the same relative position of the NL tag. Three ETO2 C -terminal HT constructs were designed to maintain the same relative position of the HT acceptor tag. ( B ) The interaction between ETO2-NHR4 and sc ( M )PPPLx4 yields a strong BRET intensity, which progressively increases with the inclusion of the NHR3 and NHR2 domains. Mutating the key tryptophan residue that interacts with the first proline of the PPPL motif (M585A) markedly decreases the BRET signal with all ETO2-HT constructs. ( C ) Truncating the PPPLx4 progressively reduces the observed BRET signal. ( D ) Introducing mutations to the ETO2-NHR2 tetramerization domain that disrupt tetramerization (M7) or dimerization (M5) decreases the BRET signal intensity ( P values reflect a comparison with the equivalent wild-type interaction). ( E ) A diagram shows the M5 and M7 mutations in the ETO2-NHR2 tetramerization domain. All measurements were performed in quadruplicate and repeated at least twice to confirm the results. P -values (<0.05=* and <0.01=**) were determined by the Student’s T-test with Welch’s correction.
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    Images

    1) Product Images from "The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex"

    Article Title: The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkaf439

    In-cell binding analysis between ETO2 and the GATAD2A (M) PPPL region. ( A ) A diagram depicts the different NanoLuc (NL) and HaloTag (HT) constructs for binding analysis by bioluminescence resonance energy transfer (NanoBRET). Six different ( M )PPPL constructs were designed, including two with the NL donor tag on the C -termini (one including the neighboring CR1 domain as a coiled-coil single chain sequence on the N -terminus, see Materials and methods). The remaining four ( M )PPPL constructs contain the NL tag on the N -terminus to allow for C -terminal truncation while maintaining the same relative position of the NL tag. Three ETO2 C -terminal HT constructs were designed to maintain the same relative position of the HT acceptor tag. ( B ) The interaction between ETO2-NHR4 and sc ( M )PPPLx4 yields a strong BRET intensity, which progressively increases with the inclusion of the NHR3 and NHR2 domains. Mutating the key tryptophan residue that interacts with the first proline of the PPPL motif (M585A) markedly decreases the BRET signal with all ETO2-HT constructs. ( C ) Truncating the PPPLx4 progressively reduces the observed BRET signal. ( D ) Introducing mutations to the ETO2-NHR2 tetramerization domain that disrupt tetramerization (M7) or dimerization (M5) decreases the BRET signal intensity ( P values reflect a comparison with the equivalent wild-type interaction). ( E ) A diagram shows the M5 and M7 mutations in the ETO2-NHR2 tetramerization domain. All measurements were performed in quadruplicate and repeated at least twice to confirm the results. P -values (<0.05=* and <0.01=**) were determined by the Student’s T-test with Welch’s correction.
    Figure Legend Snippet: In-cell binding analysis between ETO2 and the GATAD2A (M) PPPL region. ( A ) A diagram depicts the different NanoLuc (NL) and HaloTag (HT) constructs for binding analysis by bioluminescence resonance energy transfer (NanoBRET). Six different ( M )PPPL constructs were designed, including two with the NL donor tag on the C -termini (one including the neighboring CR1 domain as a coiled-coil single chain sequence on the N -terminus, see Materials and methods). The remaining four ( M )PPPL constructs contain the NL tag on the N -terminus to allow for C -terminal truncation while maintaining the same relative position of the NL tag. Three ETO2 C -terminal HT constructs were designed to maintain the same relative position of the HT acceptor tag. ( B ) The interaction between ETO2-NHR4 and sc ( M )PPPLx4 yields a strong BRET intensity, which progressively increases with the inclusion of the NHR3 and NHR2 domains. Mutating the key tryptophan residue that interacts with the first proline of the PPPL motif (M585A) markedly decreases the BRET signal with all ETO2-HT constructs. ( C ) Truncating the PPPLx4 progressively reduces the observed BRET signal. ( D ) Introducing mutations to the ETO2-NHR2 tetramerization domain that disrupt tetramerization (M7) or dimerization (M5) decreases the BRET signal intensity ( P values reflect a comparison with the equivalent wild-type interaction). ( E ) A diagram shows the M5 and M7 mutations in the ETO2-NHR2 tetramerization domain. All measurements were performed in quadruplicate and repeated at least twice to confirm the results. P -values (<0.05=* and <0.01=**) were determined by the Student’s T-test with Welch’s correction.

    Techniques Used: Binding Assay, Construct, Bioluminescence Resonance Energy Transfer, Sequencing, Residue, Comparison



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    In-cell binding analysis between ETO2 and the GATAD2A (M) PPPL region. ( A ) A diagram depicts the different <t>NanoLuc</t> (NL) <t>and</t> <t>HaloTag</t> (HT) constructs for binding analysis by bioluminescence resonance energy transfer (NanoBRET). Six different ( M )PPPL constructs were designed, including two with the NL donor tag on the C -termini (one including the neighboring CR1 domain as a coiled-coil single chain sequence on the N -terminus, see Materials and methods). The remaining four ( M )PPPL constructs contain the NL tag on the N -terminus to allow for C -terminal truncation while maintaining the same relative position of the NL tag. Three ETO2 C -terminal HT constructs were designed to maintain the same relative position of the HT acceptor tag. ( B ) The interaction between ETO2-NHR4 and sc ( M )PPPLx4 yields a strong BRET intensity, which progressively increases with the inclusion of the NHR3 and NHR2 domains. Mutating the key tryptophan residue that interacts with the first proline of the PPPL motif (M585A) markedly decreases the BRET signal with all ETO2-HT constructs. ( C ) Truncating the PPPLx4 progressively reduces the observed BRET signal. ( D ) Introducing mutations to the ETO2-NHR2 tetramerization domain that disrupt tetramerization (M7) or dimerization (M5) decreases the BRET signal intensity ( P values reflect a comparison with the equivalent wild-type interaction). ( E ) A diagram shows the M5 and M7 mutations in the ETO2-NHR2 tetramerization domain. All measurements were performed in quadruplicate and repeated at least twice to confirm the results. P -values (<0.05=* and <0.01=**) were determined by the Student’s T-test with Welch’s correction.
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    Image Search Results


    In-cell binding analysis between ETO2 and the GATAD2A (M) PPPL region. ( A ) A diagram depicts the different NanoLuc (NL) and HaloTag (HT) constructs for binding analysis by bioluminescence resonance energy transfer (NanoBRET). Six different ( M )PPPL constructs were designed, including two with the NL donor tag on the C -termini (one including the neighboring CR1 domain as a coiled-coil single chain sequence on the N -terminus, see Materials and methods). The remaining four ( M )PPPL constructs contain the NL tag on the N -terminus to allow for C -terminal truncation while maintaining the same relative position of the NL tag. Three ETO2 C -terminal HT constructs were designed to maintain the same relative position of the HT acceptor tag. ( B ) The interaction between ETO2-NHR4 and sc ( M )PPPLx4 yields a strong BRET intensity, which progressively increases with the inclusion of the NHR3 and NHR2 domains. Mutating the key tryptophan residue that interacts with the first proline of the PPPL motif (M585A) markedly decreases the BRET signal with all ETO2-HT constructs. ( C ) Truncating the PPPLx4 progressively reduces the observed BRET signal. ( D ) Introducing mutations to the ETO2-NHR2 tetramerization domain that disrupt tetramerization (M7) or dimerization (M5) decreases the BRET signal intensity ( P values reflect a comparison with the equivalent wild-type interaction). ( E ) A diagram shows the M5 and M7 mutations in the ETO2-NHR2 tetramerization domain. All measurements were performed in quadruplicate and repeated at least twice to confirm the results. P -values (<0.05=* and <0.01=**) were determined by the Student’s T-test with Welch’s correction.

    Journal: Nucleic Acids Research

    Article Title: The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex

    doi: 10.1093/nar/gkaf439

    Figure Lengend Snippet: In-cell binding analysis between ETO2 and the GATAD2A (M) PPPL region. ( A ) A diagram depicts the different NanoLuc (NL) and HaloTag (HT) constructs for binding analysis by bioluminescence resonance energy transfer (NanoBRET). Six different ( M )PPPL constructs were designed, including two with the NL donor tag on the C -termini (one including the neighboring CR1 domain as a coiled-coil single chain sequence on the N -terminus, see Materials and methods). The remaining four ( M )PPPL constructs contain the NL tag on the N -terminus to allow for C -terminal truncation while maintaining the same relative position of the NL tag. Three ETO2 C -terminal HT constructs were designed to maintain the same relative position of the HT acceptor tag. ( B ) The interaction between ETO2-NHR4 and sc ( M )PPPLx4 yields a strong BRET intensity, which progressively increases with the inclusion of the NHR3 and NHR2 domains. Mutating the key tryptophan residue that interacts with the first proline of the PPPL motif (M585A) markedly decreases the BRET signal with all ETO2-HT constructs. ( C ) Truncating the PPPLx4 progressively reduces the observed BRET signal. ( D ) Introducing mutations to the ETO2-NHR2 tetramerization domain that disrupt tetramerization (M7) or dimerization (M5) decreases the BRET signal intensity ( P values reflect a comparison with the equivalent wild-type interaction). ( E ) A diagram shows the M5 and M7 mutations in the ETO2-NHR2 tetramerization domain. All measurements were performed in quadruplicate and repeated at least twice to confirm the results. P -values (<0.05=* and <0.01=**) were determined by the Student’s T-test with Welch’s correction.

    Article Snippet: We transfected cells at ∼80% confluency in a six-well (or 12-well) cell-culture treated plates with 2 μg (or 1) and 0.2 μg (or 0.1) of HaloTag® and NanoLuc® fusion proteins using 6 μL (or 3) of Fugene HD Transfection Reagent (Promega) following the manufacturer's protocol.

    Techniques: Binding Assay, Construct, Bioluminescence Resonance Energy Transfer, Sequencing, Residue, Comparison