e1b 19kda specific antibody  (Millipore)


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    Structured Review

    Millipore e1b 19kda specific antibody
    Construction and characterization of viruses . (A) Transcriptional activity of the AFP promoter in different cell lines. The AFP promoter with an SV40 enhancer was incorporated into pGL3-basic. The relative activity of pGL3-SV40EAFP to pGL3-Control in various cell lines are presented as the mean+SD (n = 3). (B) Schematic structure of the viruses Ad.SPDD, Ad.SPDD-HCCS1, and Ad.SPDD-HCCS1. ITR, inverted terminal repeat; ψ, viral packing signal. Ad.SPDD was quadruply modified compared to the wild-type adenovirus; the modifications were the deletion of E1B19K, the deletion of E1B55K, and the deletion of 24 bp of E1A, as well as deletion of the survivin promoter controlling E1A expression. HCCS1 or HA-tagged HCCS1 in a cassette was carried by Ad.SPDD. (C) Characterization of viruses by western blot analysis. Huh-7 cells were infected with the indicated viruses, and the levels of the expressed E1A, <t>E1B</t> <t>19KDa,</t> E1B 55KDa and HA-Tag were analyzed 48 hours post infection (h.p.i), with actin as loading control. (***: P
    E1b 19kda Specific Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e1b 19kda specific antibody/product/Millipore
    Average 85 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    e1b 19kda specific antibody - by Bioz Stars, 2020-09
    85/100 stars

    Images

    1) Product Images from "HCCS1-armed, quadruple-regulated oncolytic adenovirus specific for liver cancer as a cancer targeting gene-viro-therapy strategy"

    Article Title: HCCS1-armed, quadruple-regulated oncolytic adenovirus specific for liver cancer as a cancer targeting gene-viro-therapy strategy

    Journal: Molecular Cancer

    doi: 10.1186/1476-4598-10-133

    Construction and characterization of viruses . (A) Transcriptional activity of the AFP promoter in different cell lines. The AFP promoter with an SV40 enhancer was incorporated into pGL3-basic. The relative activity of pGL3-SV40EAFP to pGL3-Control in various cell lines are presented as the mean+SD (n = 3). (B) Schematic structure of the viruses Ad.SPDD, Ad.SPDD-HCCS1, and Ad.SPDD-HCCS1. ITR, inverted terminal repeat; ψ, viral packing signal. Ad.SPDD was quadruply modified compared to the wild-type adenovirus; the modifications were the deletion of E1B19K, the deletion of E1B55K, and the deletion of 24 bp of E1A, as well as deletion of the survivin promoter controlling E1A expression. HCCS1 or HA-tagged HCCS1 in a cassette was carried by Ad.SPDD. (C) Characterization of viruses by western blot analysis. Huh-7 cells were infected with the indicated viruses, and the levels of the expressed E1A, E1B 19KDa, E1B 55KDa and HA-Tag were analyzed 48 hours post infection (h.p.i), with actin as loading control. (***: P
    Figure Legend Snippet: Construction and characterization of viruses . (A) Transcriptional activity of the AFP promoter in different cell lines. The AFP promoter with an SV40 enhancer was incorporated into pGL3-basic. The relative activity of pGL3-SV40EAFP to pGL3-Control in various cell lines are presented as the mean+SD (n = 3). (B) Schematic structure of the viruses Ad.SPDD, Ad.SPDD-HCCS1, and Ad.SPDD-HCCS1. ITR, inverted terminal repeat; ψ, viral packing signal. Ad.SPDD was quadruply modified compared to the wild-type adenovirus; the modifications were the deletion of E1B19K, the deletion of E1B55K, and the deletion of 24 bp of E1A, as well as deletion of the survivin promoter controlling E1A expression. HCCS1 or HA-tagged HCCS1 in a cassette was carried by Ad.SPDD. (C) Characterization of viruses by western blot analysis. Huh-7 cells were infected with the indicated viruses, and the levels of the expressed E1A, E1B 19KDa, E1B 55KDa and HA-Tag were analyzed 48 hours post infection (h.p.i), with actin as loading control. (***: P

    Techniques Used: Activity Assay, Modification, Expressing, Western Blot, Infection

    2) Product Images from "Transforming Potential of the Adenovirus Type 5 E4orf3 Protein"

    Article Title: Transforming Potential of the Adenovirus Type 5 E4orf3 Protein

    Journal: Journal of Virology

    doi:

    E4orf3 can bind to E1B-55kDa in transformed rat cells. (A) Expression levels of E1B-55kDa and HA-E4orf3. Total-cell extracts were prepared from the indicated cell lines. Immunoprecipitations were performed with antibodies to E1B-55kDa (2A6) and HA-E4orf3 (12CA5), respectively, and both proteins were detected in immunoprecipitates by Western blot assays using the same antibodies. (B) The same total-cell extracts were subjected to immunoprecipitation using anti-E1B-55kDa MAb 2A6. The precipitates were resolved on a 15% protein gel and transferred to a nitrocellulose membrane. The HA-tagged E4orf3 proteins were visualized with MAb 12CA5 followed by enhanced chemiluminescence. The cell line ABT27 (lane 5) was established from foci obtained after transfection of pSVHA-E4orf3 and pAd5 dl 338 Xho I-C. IgG, immunoglobulin G.
    Figure Legend Snippet: E4orf3 can bind to E1B-55kDa in transformed rat cells. (A) Expression levels of E1B-55kDa and HA-E4orf3. Total-cell extracts were prepared from the indicated cell lines. Immunoprecipitations were performed with antibodies to E1B-55kDa (2A6) and HA-E4orf3 (12CA5), respectively, and both proteins were detected in immunoprecipitates by Western blot assays using the same antibodies. (B) The same total-cell extracts were subjected to immunoprecipitation using anti-E1B-55kDa MAb 2A6. The precipitates were resolved on a 15% protein gel and transferred to a nitrocellulose membrane. The HA-tagged E4orf3 proteins were visualized with MAb 12CA5 followed by enhanced chemiluminescence. The cell line ABT27 (lane 5) was established from foci obtained after transfection of pSVHA-E4orf3 and pAd5 dl 338 Xho I-C. IgG, immunoglobulin G.

    Techniques Used: Transformation Assay, Expressing, Western Blot, Immunoprecipitation, Transfection

    Protein analysis of selected AB, ABS, ABT, and ABST cells. (A) The same amount of whole-cell extract was separated on SDS–10% polyacrylamide gels and transferred to a nitrocellulose filter by Western blotting. The same filter was then subsequently probed with anti-E1B-55kDa MAb 2A6, anti-E1A antibody M73, and anti-E1B-19kDa antibody 1G11 followed by enhanced chemiluminescence. Quantitative loading of proteins was determined by probing the filter with the anti-β-actin antibody AC-15. (B) Equal amounts of total cell extracts were subjected to immunoprecipitation using anti-p53 MAb PAb421, anti-E4orf6 MAb RSA3, anti-E4orf3 MAb 6A11, or anti-HA antibody 12CA5. The precipitates were resolved on 10 to 15% protein gels and transferred to nitrocellulose membranes. The p53 and E4orf6 proteins were visualized with antibodies CM-1 and RSA3, respectively, followed by enhanced chemiluminescence. Native E4orf3 and HA-tagged E4orf3 were detected with MAb 6A11 and the HA-specific antibody 12CA5, respectively.
    Figure Legend Snippet: Protein analysis of selected AB, ABS, ABT, and ABST cells. (A) The same amount of whole-cell extract was separated on SDS–10% polyacrylamide gels and transferred to a nitrocellulose filter by Western blotting. The same filter was then subsequently probed with anti-E1B-55kDa MAb 2A6, anti-E1A antibody M73, and anti-E1B-19kDa antibody 1G11 followed by enhanced chemiluminescence. Quantitative loading of proteins was determined by probing the filter with the anti-β-actin antibody AC-15. (B) Equal amounts of total cell extracts were subjected to immunoprecipitation using anti-p53 MAb PAb421, anti-E4orf6 MAb RSA3, anti-E4orf3 MAb 6A11, or anti-HA antibody 12CA5. The precipitates were resolved on 10 to 15% protein gels and transferred to nitrocellulose membranes. The p53 and E4orf6 proteins were visualized with antibodies CM-1 and RSA3, respectively, followed by enhanced chemiluminescence. Native E4orf3 and HA-tagged E4orf3 were detected with MAb 6A11 and the HA-specific antibody 12CA5, respectively.

    Techniques Used: Western Blot, Immunoprecipitation

    3) Product Images from "Transforming Potential of the Adenovirus Type 5 E4orf3 Protein"

    Article Title: Transforming Potential of the Adenovirus Type 5 E4orf3 Protein

    Journal: Journal of Virology

    doi:

    Focus formation by Ad5 E1, E4orf3, and E4orf6 plasmids. (A) Primary BRK cells were transfected with the indicated amounts of plasmids (micrograms of DNA), and plates were stained 21 days after transfection with crystal violet. Focus-forming activity is represented as a percentage of pAd5 Xho I-C activity. The mean and standard deviation are presented for four independent experiments. The average number of foci for pAd5 Xho I-C was 68. E1A/19k denotes plasmid pAd5 dl 338 Xho I-C, which encodes E1A and E1B-19kDa proteins. (B) Plates were stained with crystal violet; a representative plate of each transfection with pAd5 Xho I-C is shown.
    Figure Legend Snippet: Focus formation by Ad5 E1, E4orf3, and E4orf6 plasmids. (A) Primary BRK cells were transfected with the indicated amounts of plasmids (micrograms of DNA), and plates were stained 21 days after transfection with crystal violet. Focus-forming activity is represented as a percentage of pAd5 Xho I-C activity. The mean and standard deviation are presented for four independent experiments. The average number of foci for pAd5 Xho I-C was 68. E1A/19k denotes plasmid pAd5 dl 338 Xho I-C, which encodes E1A and E1B-19kDa proteins. (B) Plates were stained with crystal violet; a representative plate of each transfection with pAd5 Xho I-C is shown.

    Techniques Used: Transfection, Staining, Activity Assay, Standard Deviation, Plasmid Preparation

    Protein analysis of selected AB, ABS, ABT, and ABST cells. (A) The same amount of whole-cell extract was separated on SDS–10% polyacrylamide gels and transferred to a nitrocellulose filter by Western blotting. The same filter was then subsequently probed with anti-E1B-55kDa MAb 2A6, anti-E1A antibody M73, and anti-E1B-19kDa antibody 1G11 followed by enhanced chemiluminescence. Quantitative loading of proteins was determined by probing the filter with the anti-β-actin antibody AC-15. (B) Equal amounts of total cell extracts were subjected to immunoprecipitation using anti-p53 MAb PAb421, anti-E4orf6 MAb RSA3, anti-E4orf3 MAb 6A11, or anti-HA antibody 12CA5. The precipitates were resolved on 10 to 15% protein gels and transferred to nitrocellulose membranes. The p53 and E4orf6 proteins were visualized with antibodies CM-1 and RSA3, respectively, followed by enhanced chemiluminescence. Native E4orf3 and HA-tagged E4orf3 were detected with MAb 6A11 and the HA-specific antibody 12CA5, respectively.
    Figure Legend Snippet: Protein analysis of selected AB, ABS, ABT, and ABST cells. (A) The same amount of whole-cell extract was separated on SDS–10% polyacrylamide gels and transferred to a nitrocellulose filter by Western blotting. The same filter was then subsequently probed with anti-E1B-55kDa MAb 2A6, anti-E1A antibody M73, and anti-E1B-19kDa antibody 1G11 followed by enhanced chemiluminescence. Quantitative loading of proteins was determined by probing the filter with the anti-β-actin antibody AC-15. (B) Equal amounts of total cell extracts were subjected to immunoprecipitation using anti-p53 MAb PAb421, anti-E4orf6 MAb RSA3, anti-E4orf3 MAb 6A11, or anti-HA antibody 12CA5. The precipitates were resolved on 10 to 15% protein gels and transferred to nitrocellulose membranes. The p53 and E4orf6 proteins were visualized with antibodies CM-1 and RSA3, respectively, followed by enhanced chemiluminescence. Native E4orf3 and HA-tagged E4orf3 were detected with MAb 6A11 and the HA-specific antibody 12CA5, respectively.

    Techniques Used: Western Blot, Immunoprecipitation

    4) Product Images from "Transforming Potential of the Adenovirus Type 5 E4orf3 Protein"

    Article Title: Transforming Potential of the Adenovirus Type 5 E4orf3 Protein

    Journal: Journal of Virology

    doi:

    Protein analysis of selected AB, ABS, ABT, and ABST cells. (A) The same amount of whole-cell extract was separated on SDS–10% polyacrylamide gels and transferred to a nitrocellulose filter by Western blotting. The same filter was then subsequently probed with anti-E1B-55kDa MAb 2A6, anti-E1A antibody M73, and anti-E1B-19kDa antibody 1G11 followed by enhanced chemiluminescence. Quantitative loading of proteins was determined by probing the filter with the anti-β-actin antibody AC-15. (B) Equal amounts of total cell extracts were subjected to immunoprecipitation using anti-p53 MAb PAb421, anti-E4orf6 MAb RSA3, anti-E4orf3 MAb 6A11, or anti-HA antibody 12CA5. The precipitates were resolved on 10 to 15% protein gels and transferred to nitrocellulose membranes. The p53 and E4orf6 proteins were visualized with antibodies CM-1 and RSA3, respectively, followed by enhanced chemiluminescence. Native E4orf3 and HA-tagged E4orf3 were detected with MAb 6A11 and the HA-specific antibody 12CA5, respectively.
    Figure Legend Snippet: Protein analysis of selected AB, ABS, ABT, and ABST cells. (A) The same amount of whole-cell extract was separated on SDS–10% polyacrylamide gels and transferred to a nitrocellulose filter by Western blotting. The same filter was then subsequently probed with anti-E1B-55kDa MAb 2A6, anti-E1A antibody M73, and anti-E1B-19kDa antibody 1G11 followed by enhanced chemiluminescence. Quantitative loading of proteins was determined by probing the filter with the anti-β-actin antibody AC-15. (B) Equal amounts of total cell extracts were subjected to immunoprecipitation using anti-p53 MAb PAb421, anti-E4orf6 MAb RSA3, anti-E4orf3 MAb 6A11, or anti-HA antibody 12CA5. The precipitates were resolved on 10 to 15% protein gels and transferred to nitrocellulose membranes. The p53 and E4orf6 proteins were visualized with antibodies CM-1 and RSA3, respectively, followed by enhanced chemiluminescence. Native E4orf3 and HA-tagged E4orf3 were detected with MAb 6A11 and the HA-specific antibody 12CA5, respectively.

    Techniques Used: Western Blot, Immunoprecipitation

    Related Articles

    Incubation:

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    Article Snippet: .. A total of 40 Boehringer units of MNase (Sigma) were added, mixed by pipetting, and incubated at 20 °C for 10 minutes, with an additional mix by pipetting after 5 minutes. ..

    Article Title: The PDZ Domain of the LIM Protein Enigma Binds to ?-Tropomyosin
    Article Snippet: .. Incubation with anti-HA mouse mAb 12CA5 (BabCO, Emeryville, CA) and protein A-Sepharose (Sigma) was for 90 min at 4°C. .. Anti-tropomyosin mouse mAb T-2780 (Sigma) was used at a dilution of 1:1000 for Western blotting.

    Injection:

    Article Title: Different Transport Mechanisms in Plant and Human AMT/Rh-type Ammonium Transporters
    Article Snippet: .. Oocytes (Dumont stage V or VI) were defolliculated using collagenase 10 mg/ml (Boehringer) and trypsin inhibitor 5 mg/ml (Sigma-Aldrich) for 1–2 h and injected with ∼50 nl of cRNA (≈20 ng/per oocyte). .. Oocytes were kept after injection for 2–3 d at 16°C in ND96 (in mM): 96 NaCl, 2 KCl, 1.8 CaCl2 , 1 MgCl2 , 5 HEPES (pH 7.4), supplemented with 2.5 mM Na-pyruvate and gentamycin (20 μg/ml).

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    Millipore e1b 19kda specific antibody
    Construction and characterization of viruses . (A) Transcriptional activity of the AFP promoter in different cell lines. The AFP promoter with an SV40 enhancer was incorporated into pGL3-basic. The relative activity of pGL3-SV40EAFP to pGL3-Control in various cell lines are presented as the mean+SD (n = 3). (B) Schematic structure of the viruses Ad.SPDD, Ad.SPDD-HCCS1, and Ad.SPDD-HCCS1. ITR, inverted terminal repeat; ψ, viral packing signal. Ad.SPDD was quadruply modified compared to the wild-type adenovirus; the modifications were the deletion of E1B19K, the deletion of E1B55K, and the deletion of 24 bp of E1A, as well as deletion of the survivin promoter controlling E1A expression. HCCS1 or HA-tagged HCCS1 in a cassette was carried by Ad.SPDD. (C) Characterization of viruses by western blot analysis. Huh-7 cells were infected with the indicated viruses, and the levels of the expressed E1A, <t>E1B</t> <t>19KDa,</t> E1B 55KDa and HA-Tag were analyzed 48 hours post infection (h.p.i), with actin as loading control. (***: P
    E1b 19kda Specific Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e1b 19kda specific antibody/product/Millipore
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e1b 19kda specific antibody - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

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    Construction and characterization of viruses . (A) Transcriptional activity of the AFP promoter in different cell lines. The AFP promoter with an SV40 enhancer was incorporated into pGL3-basic. The relative activity of pGL3-SV40EAFP to pGL3-Control in various cell lines are presented as the mean+SD (n = 3). (B) Schematic structure of the viruses Ad.SPDD, Ad.SPDD-HCCS1, and Ad.SPDD-HCCS1. ITR, inverted terminal repeat; ψ, viral packing signal. Ad.SPDD was quadruply modified compared to the wild-type adenovirus; the modifications were the deletion of E1B19K, the deletion of E1B55K, and the deletion of 24 bp of E1A, as well as deletion of the survivin promoter controlling E1A expression. HCCS1 or HA-tagged HCCS1 in a cassette was carried by Ad.SPDD. (C) Characterization of viruses by western blot analysis. Huh-7 cells were infected with the indicated viruses, and the levels of the expressed E1A, E1B 19KDa, E1B 55KDa and HA-Tag were analyzed 48 hours post infection (h.p.i), with actin as loading control. (***: P

    Journal: Molecular Cancer

    Article Title: HCCS1-armed, quadruple-regulated oncolytic adenovirus specific for liver cancer as a cancer targeting gene-viro-therapy strategy

    doi: 10.1186/1476-4598-10-133

    Figure Lengend Snippet: Construction and characterization of viruses . (A) Transcriptional activity of the AFP promoter in different cell lines. The AFP promoter with an SV40 enhancer was incorporated into pGL3-basic. The relative activity of pGL3-SV40EAFP to pGL3-Control in various cell lines are presented as the mean+SD (n = 3). (B) Schematic structure of the viruses Ad.SPDD, Ad.SPDD-HCCS1, and Ad.SPDD-HCCS1. ITR, inverted terminal repeat; ψ, viral packing signal. Ad.SPDD was quadruply modified compared to the wild-type adenovirus; the modifications were the deletion of E1B19K, the deletion of E1B55K, and the deletion of 24 bp of E1A, as well as deletion of the survivin promoter controlling E1A expression. HCCS1 or HA-tagged HCCS1 in a cassette was carried by Ad.SPDD. (C) Characterization of viruses by western blot analysis. Huh-7 cells were infected with the indicated viruses, and the levels of the expressed E1A, E1B 19KDa, E1B 55KDa and HA-Tag were analyzed 48 hours post infection (h.p.i), with actin as loading control. (***: P

    Article Snippet: The E1B 55kDa-specific antibody was purchased from Oncogene (Cambridge, MA), the E1B 19kDa-specific antibody was purchased from Calbiochem (San Diego, CA), and the Hexona-specific antibody was obtained from Millipore (Billerica, MA).

    Techniques: Activity Assay, Modification, Expressing, Western Blot, Infection