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pdire vector harboring icre gene  (Addgene inc)


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    Addgene inc pdire vector harboring icre gene
    Fig. 1. A 3D ribbon model of both homo-tetramer and monomer <t>iCre</t> recombinase generated with SWISS-MODEL web server https://swissmodel.expasy.org (Waterhouse et al., 2018). The model illustrates the protein’s interaction with DNA. The active site tyrosine is marked with a black star in the C-terminal catalytic domain. B Amino acid sequence of iCre recombinase with the different domains reported. In grey the nuclear localization sequence (NLS). The red arrow indicates the split location used in (Hirrlinger et al., 2009). α-Helices are highlighted as a thicker cylinder (A-N), β-strands are labelled 1–5 and polylinker between E and F α-helices connects the N-terminal to the C-terminal of the recombinase, which contains the catalytic domain. Active-site residues are boxed; asterisks show amino acids that contact DNA in the subunit that cleaves lox site; in red boxes are highlighted the methionine residues and the position of the progressively ATG-deleted iCre isoforms, starting from the iCre sequence deleted of its first methionine (namely iCreΔ1) to that one deleted of its 6th methionine (namely iCreΔ6). (For inter pretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Pdire Vector Harboring Icre Gene, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pdire vector harboring icre gene/product/Addgene inc
    Average 92 stars, based on 21 article reviews
    pdire vector harboring icre gene - by Bioz Stars, 2026-02
    92/100 stars

    Images

    1) Product Images from "Functional study of residual iCre activity relevant for split-Cre applications"

    Article Title: Functional study of residual iCre activity relevant for split-Cre applications

    Journal: Current Research in Biotechnology

    doi: 10.1016/j.crbiot.2024.100263

    Fig. 1. A 3D ribbon model of both homo-tetramer and monomer iCre recombinase generated with SWISS-MODEL web server https://swissmodel.expasy.org (Waterhouse et al., 2018). The model illustrates the protein’s interaction with DNA. The active site tyrosine is marked with a black star in the C-terminal catalytic domain. B Amino acid sequence of iCre recombinase with the different domains reported. In grey the nuclear localization sequence (NLS). The red arrow indicates the split location used in (Hirrlinger et al., 2009). α-Helices are highlighted as a thicker cylinder (A-N), β-strands are labelled 1–5 and polylinker between E and F α-helices connects the N-terminal to the C-terminal of the recombinase, which contains the catalytic domain. Active-site residues are boxed; asterisks show amino acids that contact DNA in the subunit that cleaves lox site; in red boxes are highlighted the methionine residues and the position of the progressively ATG-deleted iCre isoforms, starting from the iCre sequence deleted of its first methionine (namely iCreΔ1) to that one deleted of its 6th methionine (namely iCreΔ6). (For inter pretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: Fig. 1. A 3D ribbon model of both homo-tetramer and monomer iCre recombinase generated with SWISS-MODEL web server https://swissmodel.expasy.org (Waterhouse et al., 2018). The model illustrates the protein’s interaction with DNA. The active site tyrosine is marked with a black star in the C-terminal catalytic domain. B Amino acid sequence of iCre recombinase with the different domains reported. In grey the nuclear localization sequence (NLS). The red arrow indicates the split location used in (Hirrlinger et al., 2009). α-Helices are highlighted as a thicker cylinder (A-N), β-strands are labelled 1–5 and polylinker between E and F α-helices connects the N-terminal to the C-terminal of the recombinase, which contains the catalytic domain. Active-site residues are boxed; asterisks show amino acids that contact DNA in the subunit that cleaves lox site; in red boxes are highlighted the methionine residues and the position of the progressively ATG-deleted iCre isoforms, starting from the iCre sequence deleted of its first methionine (namely iCreΔ1) to that one deleted of its 6th methionine (namely iCreΔ6). (For inter pretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Generated, Sequencing

    Fig. 3. Comparison of ribbon models (both homo-tetramer and monomer) for each N-terminal deleted iCre isoform generated using the resource https://swissmodel. expasy.org/ (Waterhouse et al., 2018).
    Figure Legend Snippet: Fig. 3. Comparison of ribbon models (both homo-tetramer and monomer) for each N-terminal deleted iCre isoform generated using the resource https://swissmodel. expasy.org/ (Waterhouse et al., 2018).

    Techniques Used: Comparison, Generated

    Fig. 4. A Schematic representation of the different isoforms of progressively N-terminal deleted iCre gene isoforms. Methionine residues present in the iCre cDNA, which serve as potential translation start sites, are highlighted as red bars. B Electrophoresis analysis of each isoform of iCre amplified by PCR highlighting the progressively amplicon size decrease. This confirms the successful generation of these truncated isoforms of iCre sequence. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: Fig. 4. A Schematic representation of the different isoforms of progressively N-terminal deleted iCre gene isoforms. Methionine residues present in the iCre cDNA, which serve as potential translation start sites, are highlighted as red bars. B Electrophoresis analysis of each isoform of iCre amplified by PCR highlighting the progressively amplicon size decrease. This confirms the successful generation of these truncated isoforms of iCre sequence. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Electrophoresis, Amplification, Sequencing

    Fig. 5. In vitro functional iCreΔ isoforms assay. Images of transfected HEK293T cells. The Cre-mediated recombination directly allows the expression of red fluorescent protein. Beside each line, schematic versions of the transfected constructs are shown. pIRES-eGFP was used as control of cell viability and transfection efficiency. pDIO-RFP was transfected alone to verify absence of aspecific RFP fluorescent signal. Scale bar: 100 µm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: Fig. 5. In vitro functional iCreΔ isoforms assay. Images of transfected HEK293T cells. The Cre-mediated recombination directly allows the expression of red fluorescent protein. Beside each line, schematic versions of the transfected constructs are shown. pIRES-eGFP was used as control of cell viability and transfection efficiency. pDIO-RFP was transfected alone to verify absence of aspecific RFP fluorescent signal. Scale bar: 100 µm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: In Vitro, Functional Assay, Transfection, Expressing, Construct, Control

    Fig. 6. High magnification confocal images of direct functional iCre assay. Images of co-transfected cells with bicistronic vector simultaneously expressing GFP and iCreΔ isoform, and a Cre-dependent RFP reporter plasmid. iCreΔ2-4 show residual recombinase activity and allow the co-expression of green and red fluorescent protein. DAPI was used to label nuclei Scale bar: 50 μm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: Fig. 6. High magnification confocal images of direct functional iCre assay. Images of co-transfected cells with bicistronic vector simultaneously expressing GFP and iCreΔ isoform, and a Cre-dependent RFP reporter plasmid. iCreΔ2-4 show residual recombinase activity and allow the co-expression of green and red fluorescent protein. DAPI was used to label nuclei Scale bar: 50 μm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Functional Assay, Transfection, Plasmid Preparation, Expressing, Activity Assay



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    pdire vector harboring icre gene  (Addgene inc)
    92
    Addgene inc pdire vector harboring icre gene
    Fig. 1. A 3D ribbon model of both homo-tetramer and monomer <t>iCre</t> recombinase generated with SWISS-MODEL web server https://swissmodel.expasy.org (Waterhouse et al., 2018). The model illustrates the protein’s interaction with DNA. The active site tyrosine is marked with a black star in the C-terminal catalytic domain. B Amino acid sequence of iCre recombinase with the different domains reported. In grey the nuclear localization sequence (NLS). The red arrow indicates the split location used in (Hirrlinger et al., 2009). α-Helices are highlighted as a thicker cylinder (A-N), β-strands are labelled 1–5 and polylinker between E and F α-helices connects the N-terminal to the C-terminal of the recombinase, which contains the catalytic domain. Active-site residues are boxed; asterisks show amino acids that contact DNA in the subunit that cleaves lox site; in red boxes are highlighted the methionine residues and the position of the progressively ATG-deleted iCre isoforms, starting from the iCre sequence deleted of its first methionine (namely iCreΔ1) to that one deleted of its 6th methionine (namely iCreΔ6). (For inter pretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Pdire Vector Harboring Icre Gene, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pdire vector harboring icre gene/product/Addgene inc
    Average 92 stars, based on 1 article reviews
    pdire vector harboring icre gene - by Bioz Stars, 2026-02
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    Fig. 1. A 3D ribbon model of both homo-tetramer and monomer iCre recombinase generated with SWISS-MODEL web server https://swissmodel.expasy.org (Waterhouse et al., 2018). The model illustrates the protein’s interaction with DNA. The active site tyrosine is marked with a black star in the C-terminal catalytic domain. B Amino acid sequence of iCre recombinase with the different domains reported. In grey the nuclear localization sequence (NLS). The red arrow indicates the split location used in (Hirrlinger et al., 2009). α-Helices are highlighted as a thicker cylinder (A-N), β-strands are labelled 1–5 and polylinker between E and F α-helices connects the N-terminal to the C-terminal of the recombinase, which contains the catalytic domain. Active-site residues are boxed; asterisks show amino acids that contact DNA in the subunit that cleaves lox site; in red boxes are highlighted the methionine residues and the position of the progressively ATG-deleted iCre isoforms, starting from the iCre sequence deleted of its first methionine (namely iCreΔ1) to that one deleted of its 6th methionine (namely iCreΔ6). (For inter pretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Current Research in Biotechnology

    Article Title: Functional study of residual iCre activity relevant for split-Cre applications

    doi: 10.1016/j.crbiot.2024.100263

    Figure Lengend Snippet: Fig. 1. A 3D ribbon model of both homo-tetramer and monomer iCre recombinase generated with SWISS-MODEL web server https://swissmodel.expasy.org (Waterhouse et al., 2018). The model illustrates the protein’s interaction with DNA. The active site tyrosine is marked with a black star in the C-terminal catalytic domain. B Amino acid sequence of iCre recombinase with the different domains reported. In grey the nuclear localization sequence (NLS). The red arrow indicates the split location used in (Hirrlinger et al., 2009). α-Helices are highlighted as a thicker cylinder (A-N), β-strands are labelled 1–5 and polylinker between E and F α-helices connects the N-terminal to the C-terminal of the recombinase, which contains the catalytic domain. Active-site residues are boxed; asterisks show amino acids that contact DNA in the subunit that cleaves lox site; in red boxes are highlighted the methionine residues and the position of the progressively ATG-deleted iCre isoforms, starting from the iCre sequence deleted of its first methionine (namely iCreΔ1) to that one deleted of its 6th methionine (namely iCreΔ6). (For inter pretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: PFU DNA polymerase (Promega, Madison, WI) was used in presence of the pDIRE vector harboring iCre gene (Addgene #26745) used as a template.

    Techniques: Generated, Sequencing

    Fig. 3. Comparison of ribbon models (both homo-tetramer and monomer) for each N-terminal deleted iCre isoform generated using the resource https://swissmodel. expasy.org/ (Waterhouse et al., 2018).

    Journal: Current Research in Biotechnology

    Article Title: Functional study of residual iCre activity relevant for split-Cre applications

    doi: 10.1016/j.crbiot.2024.100263

    Figure Lengend Snippet: Fig. 3. Comparison of ribbon models (both homo-tetramer and monomer) for each N-terminal deleted iCre isoform generated using the resource https://swissmodel. expasy.org/ (Waterhouse et al., 2018).

    Article Snippet: PFU DNA polymerase (Promega, Madison, WI) was used in presence of the pDIRE vector harboring iCre gene (Addgene #26745) used as a template.

    Techniques: Comparison, Generated

    Fig. 4. A Schematic representation of the different isoforms of progressively N-terminal deleted iCre gene isoforms. Methionine residues present in the iCre cDNA, which serve as potential translation start sites, are highlighted as red bars. B Electrophoresis analysis of each isoform of iCre amplified by PCR highlighting the progressively amplicon size decrease. This confirms the successful generation of these truncated isoforms of iCre sequence. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Current Research in Biotechnology

    Article Title: Functional study of residual iCre activity relevant for split-Cre applications

    doi: 10.1016/j.crbiot.2024.100263

    Figure Lengend Snippet: Fig. 4. A Schematic representation of the different isoforms of progressively N-terminal deleted iCre gene isoforms. Methionine residues present in the iCre cDNA, which serve as potential translation start sites, are highlighted as red bars. B Electrophoresis analysis of each isoform of iCre amplified by PCR highlighting the progressively amplicon size decrease. This confirms the successful generation of these truncated isoforms of iCre sequence. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: PFU DNA polymerase (Promega, Madison, WI) was used in presence of the pDIRE vector harboring iCre gene (Addgene #26745) used as a template.

    Techniques: Electrophoresis, Amplification, Sequencing

    Fig. 5. In vitro functional iCreΔ isoforms assay. Images of transfected HEK293T cells. The Cre-mediated recombination directly allows the expression of red fluorescent protein. Beside each line, schematic versions of the transfected constructs are shown. pIRES-eGFP was used as control of cell viability and transfection efficiency. pDIO-RFP was transfected alone to verify absence of aspecific RFP fluorescent signal. Scale bar: 100 µm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Current Research in Biotechnology

    Article Title: Functional study of residual iCre activity relevant for split-Cre applications

    doi: 10.1016/j.crbiot.2024.100263

    Figure Lengend Snippet: Fig. 5. In vitro functional iCreΔ isoforms assay. Images of transfected HEK293T cells. The Cre-mediated recombination directly allows the expression of red fluorescent protein. Beside each line, schematic versions of the transfected constructs are shown. pIRES-eGFP was used as control of cell viability and transfection efficiency. pDIO-RFP was transfected alone to verify absence of aspecific RFP fluorescent signal. Scale bar: 100 µm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: PFU DNA polymerase (Promega, Madison, WI) was used in presence of the pDIRE vector harboring iCre gene (Addgene #26745) used as a template.

    Techniques: In Vitro, Functional Assay, Transfection, Expressing, Construct, Control

    Fig. 6. High magnification confocal images of direct functional iCre assay. Images of co-transfected cells with bicistronic vector simultaneously expressing GFP and iCreΔ isoform, and a Cre-dependent RFP reporter plasmid. iCreΔ2-4 show residual recombinase activity and allow the co-expression of green and red fluorescent protein. DAPI was used to label nuclei Scale bar: 50 μm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Current Research in Biotechnology

    Article Title: Functional study of residual iCre activity relevant for split-Cre applications

    doi: 10.1016/j.crbiot.2024.100263

    Figure Lengend Snippet: Fig. 6. High magnification confocal images of direct functional iCre assay. Images of co-transfected cells with bicistronic vector simultaneously expressing GFP and iCreΔ isoform, and a Cre-dependent RFP reporter plasmid. iCreΔ2-4 show residual recombinase activity and allow the co-expression of green and red fluorescent protein. DAPI was used to label nuclei Scale bar: 50 μm. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: PFU DNA polymerase (Promega, Madison, WI) was used in presence of the pDIRE vector harboring iCre gene (Addgene #26745) used as a template.

    Techniques: Functional Assay, Transfection, Plasmid Preparation, Expressing, Activity Assay