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Becton Dickinson klenow dna polymerase
Klenow Dna Polymerase, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 3 article reviews
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Polymerase Chain Reaction:

Article Title: Grouping and Classifying Electrophysiologically-Defined Classes of Neocortical Neurons by Single Cell, Whole-Genome Expression Profiling
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Bioscience) and labeled with Cy3/Cy5-modified dCTP using Klenow DNA polymerase (BD Bioscience). .. The labeled samples were hybridized against a reference of amplified cDNA pooled from all of the neurons studied.

Article Title: Modelling and measuring single cell RNA expression levels find considerable transcriptional differences among phenotypically identical cells
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Bioscience – GE Healthcare) and labeled with Cy3/Cy5-modified dCTP using Klenow DNA polymerase (BD Bioscience). .. For microarray analysis of two halves of the same cell, the cell was placed in 9 ml of ice-cold stock buffer as described above, incubated for 2 min, then the lysate was divided into two parts of 4.5 μl each for global polyadenylated PCR amplification.

Article Title: Comparative evaluation of linear and exponential amplification techniques for expression profiling at the single-cell level
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Biosciences) and indirectly labeled with aminoallyl dNTP using Klenow DNA polymerase (BD Biosciences, Franklin Lakes, USA) followed by coupling with Cy3 or Cy5 NHS esters [ ]. ..

Labeling:

Article Title: Grouping and Classifying Electrophysiologically-Defined Classes of Neocortical Neurons by Single Cell, Whole-Genome Expression Profiling
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Bioscience) and labeled with Cy3/Cy5-modified dCTP using Klenow DNA polymerase (BD Bioscience). .. The labeled samples were hybridized against a reference of amplified cDNA pooled from all of the neurons studied.

Article Title: Modelling and measuring single cell RNA expression levels find considerable transcriptional differences among phenotypically identical cells
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Bioscience – GE Healthcare) and labeled with Cy3/Cy5-modified dCTP using Klenow DNA polymerase (BD Bioscience). .. For microarray analysis of two halves of the same cell, the cell was placed in 9 ml of ice-cold stock buffer as described above, incubated for 2 min, then the lysate was divided into two parts of 4.5 μl each for global polyadenylated PCR amplification.

Article Title: Comparative evaluation of linear and exponential amplification techniques for expression profiling at the single-cell level
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Biosciences) and indirectly labeled with aminoallyl dNTP using Klenow DNA polymerase (BD Biosciences, Franklin Lakes, USA) followed by coupling with Cy3 or Cy5 NHS esters [ ]. ..

Purification:

Article Title: Grouping and Classifying Electrophysiologically-Defined Classes of Neocortical Neurons by Single Cell, Whole-Genome Expression Profiling
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Bioscience) and labeled with Cy3/Cy5-modified dCTP using Klenow DNA polymerase (BD Bioscience). .. The labeled samples were hybridized against a reference of amplified cDNA pooled from all of the neurons studied.

Article Title: Modelling and measuring single cell RNA expression levels find considerable transcriptional differences among phenotypically identical cells
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Bioscience – GE Healthcare) and labeled with Cy3/Cy5-modified dCTP using Klenow DNA polymerase (BD Bioscience). .. For microarray analysis of two halves of the same cell, the cell was placed in 9 ml of ice-cold stock buffer as described above, incubated for 2 min, then the lysate was divided into two parts of 4.5 μl each for global polyadenylated PCR amplification.

Article Title: Comparative evaluation of linear and exponential amplification techniques for expression profiling at the single-cell level
Article Snippet: .. PCR products were purified with the CyScribe GFX Purification kit (Amersham Biosciences) and indirectly labeled with aminoallyl dNTP using Klenow DNA polymerase (BD Biosciences, Franklin Lakes, USA) followed by coupling with Cy3 or Cy5 NHS esters [ ]. ..

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    Becton Dickinson lexa dna binding domain
    CP2b has a very weak <t>DNA</t> binding activity but interacts with other isoforms. (A) EMSA demonstrated that recombinant GST-CP2b bound very weakly to the probe DNA, while other isoforms showed strong DNA binding activities (a). For the EMSA, increasing amounts of each recombinant CP2 isoform were incubated with the 32 P-labeled DNA probe of consensus CP2 binding sites. The highest protein levels of each CP2 isoform added to the EMSA reaction mixture (lanes 5, 10, and 15) were detected on a Coomassie blue-stained gel (b). (B) CP2b modulated DNA binding activity of other isoforms. Proteins and a DNA probe were incubated either at the same time (left two panels) or GST-CP2b was added 10 min after the incubation of GST-CP2a or-CP2c protein with DNA (right two panels). (C) The yeast two-hybrid system demonstrates that both CP2a and CP2b interact with CP2c. A yeast strain EGY48 containing the reporter gene (p8op-LacZ) was transformed with plasmids as indicated. The pB42AD CP2c plasmid contains the open reading frame of the full-length CP2c protein (aa 1 to 502) in frame with the B42 polypeptide activation domain (B42AD). The pLexA CP2aΔN, pLexA CP2bΔN, and pLexA CP2c (aa 306 to 502) contain coding regions of CP2a and CP2b N-terminal (aa 1 to 40) deletion forms, and the CP2c dimerization domain fused to the <t>LexA</t> DNA binding domain, respectively. An empty plasmid, pLexA, was a negative control. (D) In vitro binding assay confirmed the interaction between CP2b and CP2c. Each extract from 293T cells overexpressing HA-CP2a, HA-CP2b, or HA-CP2c was incubated with GST or GST-CP2c and bound to glutathione-Sepharose. Eluted materials were electrophoresed on the 10% SDS-polyacrylamide gel, and the bound CP2 proteins were visualized by immunoblotting with HA antibody. One-tenth of the amount of extract in the binding assay was used as input extracts. Mock, cell extract transfected with the CMV-HA vector as a negative control.
    Lexa Dna Binding Domain, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson α0 gene
    Coimmunoprecipitation of ICP0 and ICP0-N/X. Vero cells were infected at an MOI of 5 FFU per cell with either wild-type HSV-1, vEL0-N/X, or both viruses. At 7 h postinfection, cell lysates were prepared and proteins were immunoprecipitated as described in Materials and Methods. The antibodies (Ab) used in these immunoprecipitations were rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of ICP0, and the affinity-purified rabbit polyclonal antibody <t>α0-N18,</t> which recognizes only the NH 2 -terminal 18 aa of wild-type ICP0. ICP0 and ICP0-N/X were detected by Western blotting using CLU7. IgG, immunoglobulin G.
    α0 Gene, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson human multiple tissue expression array bd mte
    Coimmunoprecipitation of ICP0 and ICP0-N/X. Vero cells were infected at an MOI of 5 FFU per cell with either wild-type HSV-1, vEL0-N/X, or both viruses. At 7 h postinfection, cell lysates were prepared and proteins were immunoprecipitated as described in Materials and Methods. The antibodies (Ab) used in these immunoprecipitations were rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of ICP0, and the affinity-purified rabbit polyclonal antibody <t>α0-N18,</t> which recognizes only the NH 2 -terminal 18 aa of wild-type ICP0. ICP0 and ICP0-N/X were detected by Western blotting using CLU7. IgG, immunoglobulin G.
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    Becton Dickinson latex slide agglutination test
    Coimmunoprecipitation of ICP0 and ICP0-N/X. Vero cells were infected at an MOI of 5 FFU per cell with either wild-type HSV-1, vEL0-N/X, or both viruses. At 7 h postinfection, cell lysates were prepared and proteins were immunoprecipitated as described in Materials and Methods. The antibodies (Ab) used in these immunoprecipitations were rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of ICP0, and the affinity-purified rabbit polyclonal antibody <t>α0-N18,</t> which recognizes only the NH 2 -terminal 18 aa of wild-type ICP0. ICP0 and ICP0-N/X were detected by Western blotting using CLU7. IgG, immunoglobulin G.
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    CP2b has a very weak DNA binding activity but interacts with other isoforms. (A) EMSA demonstrated that recombinant GST-CP2b bound very weakly to the probe DNA, while other isoforms showed strong DNA binding activities (a). For the EMSA, increasing amounts of each recombinant CP2 isoform were incubated with the 32 P-labeled DNA probe of consensus CP2 binding sites. The highest protein levels of each CP2 isoform added to the EMSA reaction mixture (lanes 5, 10, and 15) were detected on a Coomassie blue-stained gel (b). (B) CP2b modulated DNA binding activity of other isoforms. Proteins and a DNA probe were incubated either at the same time (left two panels) or GST-CP2b was added 10 min after the incubation of GST-CP2a or-CP2c protein with DNA (right two panels). (C) The yeast two-hybrid system demonstrates that both CP2a and CP2b interact with CP2c. A yeast strain EGY48 containing the reporter gene (p8op-LacZ) was transformed with plasmids as indicated. The pB42AD CP2c plasmid contains the open reading frame of the full-length CP2c protein (aa 1 to 502) in frame with the B42 polypeptide activation domain (B42AD). The pLexA CP2aΔN, pLexA CP2bΔN, and pLexA CP2c (aa 306 to 502) contain coding regions of CP2a and CP2b N-terminal (aa 1 to 40) deletion forms, and the CP2c dimerization domain fused to the LexA DNA binding domain, respectively. An empty plasmid, pLexA, was a negative control. (D) In vitro binding assay confirmed the interaction between CP2b and CP2c. Each extract from 293T cells overexpressing HA-CP2a, HA-CP2b, or HA-CP2c was incubated with GST or GST-CP2c and bound to glutathione-Sepharose. Eluted materials were electrophoresed on the 10% SDS-polyacrylamide gel, and the bound CP2 proteins were visualized by immunoblotting with HA antibody. One-tenth of the amount of extract in the binding assay was used as input extracts. Mock, cell extract transfected with the CMV-HA vector as a negative control.

    Journal: Molecular and Cellular Biology

    Article Title: Erythroid Cell-Specific ?-Globin Gene Regulation by the CP2 Transcription Factor Family

    doi: 10.1128/MCB.25.14.6005-6020.2005

    Figure Lengend Snippet: CP2b has a very weak DNA binding activity but interacts with other isoforms. (A) EMSA demonstrated that recombinant GST-CP2b bound very weakly to the probe DNA, while other isoforms showed strong DNA binding activities (a). For the EMSA, increasing amounts of each recombinant CP2 isoform were incubated with the 32 P-labeled DNA probe of consensus CP2 binding sites. The highest protein levels of each CP2 isoform added to the EMSA reaction mixture (lanes 5, 10, and 15) were detected on a Coomassie blue-stained gel (b). (B) CP2b modulated DNA binding activity of other isoforms. Proteins and a DNA probe were incubated either at the same time (left two panels) or GST-CP2b was added 10 min after the incubation of GST-CP2a or-CP2c protein with DNA (right two panels). (C) The yeast two-hybrid system demonstrates that both CP2a and CP2b interact with CP2c. A yeast strain EGY48 containing the reporter gene (p8op-LacZ) was transformed with plasmids as indicated. The pB42AD CP2c plasmid contains the open reading frame of the full-length CP2c protein (aa 1 to 502) in frame with the B42 polypeptide activation domain (B42AD). The pLexA CP2aΔN, pLexA CP2bΔN, and pLexA CP2c (aa 306 to 502) contain coding regions of CP2a and CP2b N-terminal (aa 1 to 40) deletion forms, and the CP2c dimerization domain fused to the LexA DNA binding domain, respectively. An empty plasmid, pLexA, was a negative control. (D) In vitro binding assay confirmed the interaction between CP2b and CP2c. Each extract from 293T cells overexpressing HA-CP2a, HA-CP2b, or HA-CP2c was incubated with GST or GST-CP2c and bound to glutathione-Sepharose. Eluted materials were electrophoresed on the 10% SDS-polyacrylamide gel, and the bound CP2 proteins were visualized by immunoblotting with HA antibody. One-tenth of the amount of extract in the binding assay was used as input extracts. Mock, cell extract transfected with the CMV-HA vector as a negative control.

    Article Snippet: These PCR products were subcloned into the EcoRI/XhoI site of the pLexA vector in frame with the LexA-DNA binding domain (LexA BD).

    Techniques: Binding Assay, Activity Assay, Recombinant, Incubation, Labeling, Staining, Transformation Assay, Plasmid Preparation, Activation Assay, Negative Control, In Vitro, Transfection

    Coimmunoprecipitation of ICP0 and ICP0-N/X. Vero cells were infected at an MOI of 5 FFU per cell with either wild-type HSV-1, vEL0-N/X, or both viruses. At 7 h postinfection, cell lysates were prepared and proteins were immunoprecipitated as described in Materials and Methods. The antibodies (Ab) used in these immunoprecipitations were rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of ICP0, and the affinity-purified rabbit polyclonal antibody α0-N18, which recognizes only the NH 2 -terminal 18 aa of wild-type ICP0. ICP0 and ICP0-N/X were detected by Western blotting using CLU7. IgG, immunoglobulin G.

    Journal: Journal of Virology

    Article Title: The NH2 Terminus of the Herpes Simplex Virus Type 1 Regulatory Protein ICP0 Contains a Promoter-Specific Transcription Activation Domain

    doi:

    Figure Lengend Snippet: Coimmunoprecipitation of ICP0 and ICP0-N/X. Vero cells were infected at an MOI of 5 FFU per cell with either wild-type HSV-1, vEL0-N/X, or both viruses. At 7 h postinfection, cell lysates were prepared and proteins were immunoprecipitated as described in Materials and Methods. The antibodies (Ab) used in these immunoprecipitations were rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of ICP0, and the affinity-purified rabbit polyclonal antibody α0-N18, which recognizes only the NH 2 -terminal 18 aa of wild-type ICP0. ICP0 and ICP0-N/X were detected by Western blotting using CLU7. IgG, immunoglobulin G.

    Article Snippet: Plasmid pJY3 (GAL4-BD–ICP0 aa 1 to 105) was constructed by deletion of the Xho I- Sal I fragment of the α0 gene from pXW2. pJY4 (GAL4-BD–ICP0 aa 1 to 212) was constructed by deletion of the Asp 718- Sal I fragment of pXW2. pJY7 (GAL4-BD–ICP0 aa 105 to 212) was constructed by insertion of the Xho I- Pst I fragment of pJY4 into pGBT9 digested with Sal I and Pst I. Plasmid pCPC-YGal03-F (GAL4-BD–ICP0 aa 394 to 775) was constructed by deletion of the Eco RI- Not I fragment of pXW2.

    Techniques: Infection, Immunoprecipitation, Affinity Purification, Western Blot

    Intranuclear distribution of ICP0 and ICP0-N/X in infected and transfected cells. Vero cells were infected with wild-type HSV-1 strain 17 (A) or the α0 mutant vEL0-N/X (B) or were transfected with plasmids encoding HSV-1 ICP0 (C), ICP0-N/X (D), or both proteins (E and F). At 7 h postinfection or 48 h posttransfection, wild-type ICP0 and the NH 2 -terminal deletion mutant ICP0-N/X were detected by indirect immunofluorescence using rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of HSV-1 ICP0 (A to D), the affinity-purified rabbit polyclonal antibody α0-N18, which recognizes only the NH 2 -terminal 18 aa acids of HSV-1 ICP0 and thus fails to recognize ICP0-N/X (E), or the anti-ICP0 mouse monoclonal antibody H1083, which recognizes both ICP0 and ICP0-N/X (F). Panels E and F show the same field of cells. The secondary antibodies used in this analysis were coupled to either fluorescein isothiocyanate (A to E) or rhodamine (F).

    Journal: Journal of Virology

    Article Title: The NH2 Terminus of the Herpes Simplex Virus Type 1 Regulatory Protein ICP0 Contains a Promoter-Specific Transcription Activation Domain

    doi:

    Figure Lengend Snippet: Intranuclear distribution of ICP0 and ICP0-N/X in infected and transfected cells. Vero cells were infected with wild-type HSV-1 strain 17 (A) or the α0 mutant vEL0-N/X (B) or were transfected with plasmids encoding HSV-1 ICP0 (C), ICP0-N/X (D), or both proteins (E and F). At 7 h postinfection or 48 h posttransfection, wild-type ICP0 and the NH 2 -terminal deletion mutant ICP0-N/X were detected by indirect immunofluorescence using rabbit polyclonal antibody CLU7, which recognizes epitopes between aa 312 and 400 of HSV-1 ICP0 (A to D), the affinity-purified rabbit polyclonal antibody α0-N18, which recognizes only the NH 2 -terminal 18 aa acids of HSV-1 ICP0 and thus fails to recognize ICP0-N/X (E), or the anti-ICP0 mouse monoclonal antibody H1083, which recognizes both ICP0 and ICP0-N/X (F). Panels E and F show the same field of cells. The secondary antibodies used in this analysis were coupled to either fluorescein isothiocyanate (A to E) or rhodamine (F).

    Article Snippet: Plasmid pJY3 (GAL4-BD–ICP0 aa 1 to 105) was constructed by deletion of the Xho I- Sal I fragment of the α0 gene from pXW2. pJY4 (GAL4-BD–ICP0 aa 1 to 212) was constructed by deletion of the Asp 718- Sal I fragment of pXW2. pJY7 (GAL4-BD–ICP0 aa 105 to 212) was constructed by insertion of the Xho I- Pst I fragment of pJY4 into pGBT9 digested with Sal I and Pst I. Plasmid pCPC-YGal03-F (GAL4-BD–ICP0 aa 394 to 775) was constructed by deletion of the Eco RI- Not I fragment of pXW2.

    Techniques: Infection, Transfection, Mutagenesis, Immunofluorescence, Affinity Purification

    Activation of HSV-1 promoters by wild-type and mutant ICP0. Vero cells were cotransfected with plasmids (1 μg) directing the expression of wild-type HSV-1 ICP0, or the indicated mutant ICP0 proteins, and the appropriate reporter plasmids (1 μg). ICP0-N/X lacks aa 3 to 104 of ICP0. ICP0-TIF contains the HSV-1 αTIF-AD in place of aa 2 to 104 of ICP0. Reporter plasmids direct expression of the firefly luciferase gene under the control of the α4 (4p-LUC), α27 (27p-LUC), α22/47 (22/47p-LUC), α0 (0p-LUC), TK (TK-LUC), or gC (gC-LUC) promoter from HSV-1. Total cell extracts were prepared at 48 h posttransfection, and luciferase activities were quantified as described in Materials and Methods. Cells transfected with reporter plasmids only are indicated (No Effector). Levels of transcriptional activation are expressed relative to the basal expression levels derived for each reporter plasmid.

    Journal: Journal of Virology

    Article Title: The NH2 Terminus of the Herpes Simplex Virus Type 1 Regulatory Protein ICP0 Contains a Promoter-Specific Transcription Activation Domain

    doi:

    Figure Lengend Snippet: Activation of HSV-1 promoters by wild-type and mutant ICP0. Vero cells were cotransfected with plasmids (1 μg) directing the expression of wild-type HSV-1 ICP0, or the indicated mutant ICP0 proteins, and the appropriate reporter plasmids (1 μg). ICP0-N/X lacks aa 3 to 104 of ICP0. ICP0-TIF contains the HSV-1 αTIF-AD in place of aa 2 to 104 of ICP0. Reporter plasmids direct expression of the firefly luciferase gene under the control of the α4 (4p-LUC), α27 (27p-LUC), α22/47 (22/47p-LUC), α0 (0p-LUC), TK (TK-LUC), or gC (gC-LUC) promoter from HSV-1. Total cell extracts were prepared at 48 h posttransfection, and luciferase activities were quantified as described in Materials and Methods. Cells transfected with reporter plasmids only are indicated (No Effector). Levels of transcriptional activation are expressed relative to the basal expression levels derived for each reporter plasmid.

    Article Snippet: Plasmid pJY3 (GAL4-BD–ICP0 aa 1 to 105) was constructed by deletion of the Xho I- Sal I fragment of the α0 gene from pXW2. pJY4 (GAL4-BD–ICP0 aa 1 to 212) was constructed by deletion of the Asp 718- Sal I fragment of pXW2. pJY7 (GAL4-BD–ICP0 aa 105 to 212) was constructed by insertion of the Xho I- Pst I fragment of pJY4 into pGBT9 digested with Sal I and Pst I. Plasmid pCPC-YGal03-F (GAL4-BD–ICP0 aa 394 to 775) was constructed by deletion of the Eco RI- Not I fragment of pXW2.

    Techniques: Activation Assay, Mutagenesis, Expressing, Luciferase, Transfection, Derivative Assay, Plasmid Preparation

    Wild-type and mutant herpesvirus plaque sizes. Vero cells were infected with the indicated wild-type and mutant herpesviruses at an MOI of 0.001. At 60 h postinfection, infected cell monolayers were fixed with 90% methanol and stained with 1% crystal violet. (A) Representative plaques photographed by standard techniques; (B) plaque sizes for wild-type HSV-1, the α0 cDNA virus vCPc0, and the α0 mutants vEL0-N/X and dl 1403, expressed as the averages of 40 measurements per virus. The average plaque sizes are expressed relative to that of wild-type HSV-1 strain 17.

    Journal: Journal of Virology

    Article Title: The NH2 Terminus of the Herpes Simplex Virus Type 1 Regulatory Protein ICP0 Contains a Promoter-Specific Transcription Activation Domain

    doi:

    Figure Lengend Snippet: Wild-type and mutant herpesvirus plaque sizes. Vero cells were infected with the indicated wild-type and mutant herpesviruses at an MOI of 0.001. At 60 h postinfection, infected cell monolayers were fixed with 90% methanol and stained with 1% crystal violet. (A) Representative plaques photographed by standard techniques; (B) plaque sizes for wild-type HSV-1, the α0 cDNA virus vCPc0, and the α0 mutants vEL0-N/X and dl 1403, expressed as the averages of 40 measurements per virus. The average plaque sizes are expressed relative to that of wild-type HSV-1 strain 17.

    Article Snippet: Plasmid pJY3 (GAL4-BD–ICP0 aa 1 to 105) was constructed by deletion of the Xho I- Sal I fragment of the α0 gene from pXW2. pJY4 (GAL4-BD–ICP0 aa 1 to 212) was constructed by deletion of the Asp 718- Sal I fragment of pXW2. pJY7 (GAL4-BD–ICP0 aa 105 to 212) was constructed by insertion of the Xho I- Pst I fragment of pJY4 into pGBT9 digested with Sal I and Pst I. Plasmid pCPC-YGal03-F (GAL4-BD–ICP0 aa 394 to 775) was constructed by deletion of the Eco RI- Not I fragment of pXW2.

    Techniques: Mutagenesis, Infection, Staining