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sgrna scaffold  (Addgene inc)


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    Structured Review

    Addgene inc sgrna scaffold
    Z7 enhances DNA binding and cleavage activity <t>of</t> <t>AtCas9</t> at low magnesium condition. (a) In vitro cleavage assay of WT and Z7 proteins with different concentrations of Mg 2+ (0.5, 1, 2, 5 mM). Three target loci ( Spacer-21a , CTNNB1-10g , and VEGFA-11g ) were tested. (b) Temperature-dependent cleavage efficiency of WT and Z7. (c) Thermal shift analysis of melting temperatures of the AtCas9 proteins. (d-e) EMSA analysis of binding affinities between Cas9 variants and <t>sgRNA</t> (d), or Cas9 RNP complexes with DNA substrates (e), under the indicated magnesium concentrations.
    Sgrna Scaffold, supplied by Addgene inc, used in various techniques. Bioz Stars score: 96/100, based on 444 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sgrna+cloning+vector/pmc12634846-215-15-21?v=Addgene+inc
    Average 96 stars, based on 444 article reviews
    sgrna scaffold - by Bioz Stars, 2026-06
    96/100 stars

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    1) Product Images from "Loop engineering of AtCas9 for effective and broad genome editing"

    Article Title: Loop engineering of AtCas9 for effective and broad genome editing

    Journal: Cell Insight

    doi: 10.1016/j.cellin.2025.100286

    Z7 enhances DNA binding and cleavage activity of AtCas9 at low magnesium condition. (a) In vitro cleavage assay of WT and Z7 proteins with different concentrations of Mg 2+ (0.5, 1, 2, 5 mM). Three target loci ( Spacer-21a , CTNNB1-10g , and VEGFA-11g ) were tested. (b) Temperature-dependent cleavage efficiency of WT and Z7. (c) Thermal shift analysis of melting temperatures of the AtCas9 proteins. (d-e) EMSA analysis of binding affinities between Cas9 variants and sgRNA (d), or Cas9 RNP complexes with DNA substrates (e), under the indicated magnesium concentrations.
    Figure Legend Snippet: Z7 enhances DNA binding and cleavage activity of AtCas9 at low magnesium condition. (a) In vitro cleavage assay of WT and Z7 proteins with different concentrations of Mg 2+ (0.5, 1, 2, 5 mM). Three target loci ( Spacer-21a , CTNNB1-10g , and VEGFA-11g ) were tested. (b) Temperature-dependent cleavage efficiency of WT and Z7. (c) Thermal shift analysis of melting temperatures of the AtCas9 proteins. (d-e) EMSA analysis of binding affinities between Cas9 variants and sgRNA (d), or Cas9 RNP complexes with DNA substrates (e), under the indicated magnesium concentrations.

    Techniques Used: Binding Assay, Activity Assay, In Vitro, Cleavage Assay

    Structure-guided protein engineering improves the editing efficiency of AtCas9 . (a) Schematic representation of sgRNA: DNA target recognition by AtCas9 variants. Residue substitutions in the E535 and E5116 variants are highlighted. (b) Adenine base editing efficiencies of AtCas9 mutants at C-myc-41g and CTNNB1-10g target sites. (c) Solvent-accessible surface area (SASA) analysis of interactions between different AtCas9 variants and nucleic acids, reflecting changes in protein–nucleic acid interface accessibility. (d) (left) A-to-G editing efficiencies of wildtype and AtCas9 E5116 mutant. (right) Median fold change of editing efficiency. Data were normalized to WT AtCas9-ABE. For (b) and (d), data are mean ± SD of n = 3 biologically independent experiments. Statistical significance was determined by unpaired t -test (∗ p ​< ​0.033, ∗∗∗ p ​< ​0.001). Each dot represents one biological experiment.
    Figure Legend Snippet: Structure-guided protein engineering improves the editing efficiency of AtCas9 . (a) Schematic representation of sgRNA: DNA target recognition by AtCas9 variants. Residue substitutions in the E535 and E5116 variants are highlighted. (b) Adenine base editing efficiencies of AtCas9 mutants at C-myc-41g and CTNNB1-10g target sites. (c) Solvent-accessible surface area (SASA) analysis of interactions between different AtCas9 variants and nucleic acids, reflecting changes in protein–nucleic acid interface accessibility. (d) (left) A-to-G editing efficiencies of wildtype and AtCas9 E5116 mutant. (right) Median fold change of editing efficiency. Data were normalized to WT AtCas9-ABE. For (b) and (d), data are mean ± SD of n = 3 biologically independent experiments. Statistical significance was determined by unpaired t -test (∗ p ​< ​0.033, ∗∗∗ p ​< ​0.001). Each dot represents one biological experiment.

    Techniques Used: Drug discovery, Residue, Solvent, Mutagenesis



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    Image Search Results


    Z7 enhances DNA binding and cleavage activity of AtCas9 at low magnesium condition. (a) In vitro cleavage assay of WT and Z7 proteins with different concentrations of Mg 2+ (0.5, 1, 2, 5 mM). Three target loci ( Spacer-21a , CTNNB1-10g , and VEGFA-11g ) were tested. (b) Temperature-dependent cleavage efficiency of WT and Z7. (c) Thermal shift analysis of melting temperatures of the AtCas9 proteins. (d-e) EMSA analysis of binding affinities between Cas9 variants and sgRNA (d), or Cas9 RNP complexes with DNA substrates (e), under the indicated magnesium concentrations.

    Journal: Cell Insight

    Article Title: Loop engineering of AtCas9 for effective and broad genome editing

    doi: 10.1016/j.cellin.2025.100286

    Figure Lengend Snippet: Z7 enhances DNA binding and cleavage activity of AtCas9 at low magnesium condition. (a) In vitro cleavage assay of WT and Z7 proteins with different concentrations of Mg 2+ (0.5, 1, 2, 5 mM). Three target loci ( Spacer-21a , CTNNB1-10g , and VEGFA-11g ) were tested. (b) Temperature-dependent cleavage efficiency of WT and Z7. (c) Thermal shift analysis of melting temperatures of the AtCas9 proteins. (d-e) EMSA analysis of binding affinities between Cas9 variants and sgRNA (d), or Cas9 RNP complexes with DNA substrates (e), under the indicated magnesium concentrations.

    Article Snippet: A U6 promoter-driven AtCas9 sgRNA mammalian expression plasmid (designated Gcl203) was created by replacing the sgRNA scaffold in the gRNA_cloning Vector (Addgene plasmid 41824) with the AtCas9 sgRNA optimized scaffold.

    Techniques: Binding Assay, Activity Assay, In Vitro, Cleavage Assay

    Structure-guided protein engineering improves the editing efficiency of AtCas9 . (a) Schematic representation of sgRNA: DNA target recognition by AtCas9 variants. Residue substitutions in the E535 and E5116 variants are highlighted. (b) Adenine base editing efficiencies of AtCas9 mutants at C-myc-41g and CTNNB1-10g target sites. (c) Solvent-accessible surface area (SASA) analysis of interactions between different AtCas9 variants and nucleic acids, reflecting changes in protein–nucleic acid interface accessibility. (d) (left) A-to-G editing efficiencies of wildtype and AtCas9 E5116 mutant. (right) Median fold change of editing efficiency. Data were normalized to WT AtCas9-ABE. For (b) and (d), data are mean ± SD of n = 3 biologically independent experiments. Statistical significance was determined by unpaired t -test (∗ p ​< ​0.033, ∗∗∗ p ​< ​0.001). Each dot represents one biological experiment.

    Journal: Cell Insight

    Article Title: Loop engineering of AtCas9 for effective and broad genome editing

    doi: 10.1016/j.cellin.2025.100286

    Figure Lengend Snippet: Structure-guided protein engineering improves the editing efficiency of AtCas9 . (a) Schematic representation of sgRNA: DNA target recognition by AtCas9 variants. Residue substitutions in the E535 and E5116 variants are highlighted. (b) Adenine base editing efficiencies of AtCas9 mutants at C-myc-41g and CTNNB1-10g target sites. (c) Solvent-accessible surface area (SASA) analysis of interactions between different AtCas9 variants and nucleic acids, reflecting changes in protein–nucleic acid interface accessibility. (d) (left) A-to-G editing efficiencies of wildtype and AtCas9 E5116 mutant. (right) Median fold change of editing efficiency. Data were normalized to WT AtCas9-ABE. For (b) and (d), data are mean ± SD of n = 3 biologically independent experiments. Statistical significance was determined by unpaired t -test (∗ p ​< ​0.033, ∗∗∗ p ​< ​0.001). Each dot represents one biological experiment.

    Article Snippet: A U6 promoter-driven AtCas9 sgRNA mammalian expression plasmid (designated Gcl203) was created by replacing the sgRNA scaffold in the gRNA_cloning Vector (Addgene plasmid 41824) with the AtCas9 sgRNA optimized scaffold.

    Techniques: Drug discovery, Residue, Solvent, Mutagenesis