e1b Search Results


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  • 99
    ATCC cell lines e1a e1b trans complementing hek 293 cell line
    Cell Lines E1a E1b Trans Complementing Hek 293 Cell Line, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher rabbit serum e1b
    Rabbit Serum E1b, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Stratagene minimal e1b promoter luciferase gene
    Minimal E1b Promoter Luciferase Gene, supplied by Stratagene, used in various techniques. Bioz Stars score: 88/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Genewiz e1b gene
    Clusters of coregulated cellular RNAs 30 h after infection with Ad5 or <t>E1B</t> mutants. The expression profiles of significantly regulated genes were clustered into eight distinct groups with similar expression response profiles across the different Ad5 genotypes as described in Materials and Methods. Each cluster was searched for statistically significant enrichment of genes that code for proteins with common functions ( P values are Bonferroni corrected for multiple hypothesis testing). GO terms enriched in clusters 2, 3, and 4 are shown at right, with the corresponding P values. Genes that increased and decreased in expression are shown in yellow and blue, respectively, as indicated on the scale bar. hpi, hours postinfection.
    E1b Gene, supplied by Genewiz, used in various techniques. Bioz Stars score: 85/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    ZIRC Inc uas e1b
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Uas E1b, supplied by ZIRC Inc, used in various techniques. Bioz Stars score: 86/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Cell Signaling Technology Inc bcl2 adenovirus e1b 19
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Bcl2 Adenovirus E1b 19, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cell Signaling Technology Inc bcl 2 adenovirus e1b 19k
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Bcl 2 Adenovirus E1b 19k, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bethyl rabbit anti e1b ap5 antibody affinity purified
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Rabbit Anti E1b Ap5 Antibody Affinity Purified, supplied by Bethyl, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Onyx Pharmaceuticals e1b 55 kda gene deleted ad5 mutant dl1520
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    E1b 55 Kda Gene Deleted Ad5 Mutant Dl1520, supplied by Onyx Pharmaceuticals, used in various techniques. Bioz Stars score: 88/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Addgene inc ac ds e1b egfp vector
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Ac Ds E1b Egfp Vector, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam anti bcl2 adenovirus e1b 19 kda interacting protein 3
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Anti Bcl2 Adenovirus E1b 19 Kda Interacting Protein 3, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Calbiotech anti adenovirus type 5 e1b 55k ab 1 rat monoclonal antibody
    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × <t>UAS:smoa1-EGFP)</t> and the <t>Tg(UAS-E1b:nfsB-mCherry)</t> c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).
    Anti Adenovirus Type 5 E1b 55k Ab 1 Rat Monoclonal Antibody, supplied by Calbiotech, 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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    92
    Abcam anti e1b ap5 antibody
    KSHV ORF57 interacts with PABPC1. (A) ORF57 interacts with PABPC1, but not with <t>E1B-AP5,</t> as shown by coimmunoprecipitation assays. Total cell extracts from TREx BCBL1-Rta cells induced by Dox (1 μg/ml) and treated with a mixture of RNase A and T1 were immunoprecipitated with preimmune mouse IgG- or monoclonal anti-ORF57 antibody-coated beads and examined for PABPC1 and E1B-AP5 by Western blotting (left). Conversely, the same extracts treated with a mixture of RNase A and T1 were immunoprecipitated with nonspecific rabbit IgG- or polyclonal anti-PABPC1 or anti-E1B-AP5 antibody-coated beads and blotted for ORF57 by Western blotting (right). (B) PABPC1 directly interacts with ORF57, as shown by GST pulldown assays. Full-length PABPC1 protein with an N-terminal GST tag or untagged GST was immobilized on glutathione-Sepharose 4B beads and incubated at 4°C overnight in IP buffer complemented with KSHV ORF57 protein containing a C-terminal FLAG tag that was expressed from baculovirus. The glutathione-Sepharose 4B beads without any GST protein were used as an additional negative control. After binding, the beads were washed five times with IP buffer, resuspended in 2× SDS sample buffer, and analyzed by Western blotting with two antibodies, an anti-GST antibody recognizing PABPC1 and an anti-FLAG antibody that recognizes the epitope-tagged ORF57.
    Anti E1b Ap5 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti e1b ap5
    Identification of nuclear transport factor 2 (NTF2)-like export protein 1 (NXT1) as a binding partner of influenza nucleoprotein (NP). ( A ) NP-FLAG or FLAG- non-structural 1 (NS1) protein was immobilized on anti-FLAG agarose beads and co-incubated with HeLa whole cell lysate overnight at 4 °C. The beads were collected, washed, and subjected to western blot (WB) analysis with anti-NXT1, anti-NUP153, anti-NUP98, anti-NUP62, <t>anti-E1B-AP5,</t> anti-CRM1, or anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials. Black arrowheads indicate specific binding. H and L indicate the heavy and light chains of the agarose-conjugated anti-FLAG antibody; ( B ) Human embryonic kidney (HEK293T) cells were transfected with NP-FLAG/pCAGGS and HA-NXT1/pCAGGS plasmids for 48 h, lysed, and incubated with anti-FLAG agarose beads overnight at 4 °C. The agarose beads were collected, washed, and subjected to WB analysis with anti- hemagglutinin (HA) and anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials; ( C ) HA-NXT1 protein was immobilized on anti-HA agarose beads and co-incubated with purified NP-FLAG protein overnight at 4 °C. The beads were collected, washed, and subjected to WB analysis with anti-FLAG and anti-HA antibodies. Data shown are the results of one representative experiment from three independent trials.
    Anti E1b Ap5, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Abcam bcl 2 adenovirus e1b 19 kda interacting protein 3 like bnip3
    Identification of nuclear transport factor 2 (NTF2)-like export protein 1 (NXT1) as a binding partner of influenza nucleoprotein (NP). ( A ) NP-FLAG or FLAG- non-structural 1 (NS1) protein was immobilized on anti-FLAG agarose beads and co-incubated with HeLa whole cell lysate overnight at 4 °C. The beads were collected, washed, and subjected to western blot (WB) analysis with anti-NXT1, anti-NUP153, anti-NUP98, anti-NUP62, <t>anti-E1B-AP5,</t> anti-CRM1, or anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials. Black arrowheads indicate specific binding. H and L indicate the heavy and light chains of the agarose-conjugated anti-FLAG antibody; ( B ) Human embryonic kidney (HEK293T) cells were transfected with NP-FLAG/pCAGGS and HA-NXT1/pCAGGS plasmids for 48 h, lysed, and incubated with anti-FLAG agarose beads overnight at 4 °C. The agarose beads were collected, washed, and subjected to WB analysis with anti- hemagglutinin (HA) and anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials; ( C ) HA-NXT1 protein was immobilized on anti-HA agarose beads and co-incubated with purified NP-FLAG protein overnight at 4 °C. The beads were collected, washed, and subjected to WB analysis with anti-FLAG and anti-HA antibodies. Data shown are the results of one representative experiment from three independent trials.
    Bcl 2 Adenovirus E1b 19 Kda Interacting Protein 3 Like Bnip3, supplied by Abcam, used in various techniques. Bioz Stars score: 96/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Santa Cruz Biotechnology bcl 2 adenovirus e1b 19 kda interacting protein 3
    Western blots of BNIP3, BNIP3 L, HIF-1α and LC3II. BNIP3, <t>Bcl-2/adenovirus</t> E1B <t>19-kDa</t> interacting protein 3; BNIP3 L, BNIP3 like; HIF-1α, hypoxia-inducible factor 1α; LC3II, microtubule-associated protein 1A/1B light chain 3B; IR, ischemia-reperfusion; pre-LD, low-dose dexmedetomidine preconditioning; pre-HD, high-dose dexmedetomidine preconditioning; post-LD, low-dose dexmedetomidine postconditioning; post-HD, high-dose dexmedetomidine postconditioning.
    Bcl 2 Adenovirus E1b 19 Kda Interacting Protein 3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc bcl2 adenovirus e1b 19 kda interacting protein 3
    Western blots of BNIP3, BNIP3 L, HIF-1α and LC3II. BNIP3, <t>Bcl-2/adenovirus</t> E1B <t>19-kDa</t> interacting protein 3; BNIP3 L, BNIP3 like; HIF-1α, hypoxia-inducible factor 1α; LC3II, microtubule-associated protein 1A/1B light chain 3B; IR, ischemia-reperfusion; pre-LD, low-dose dexmedetomidine preconditioning; pre-HD, high-dose dexmedetomidine preconditioning; post-LD, low-dose dexmedetomidine postconditioning; post-HD, high-dose dexmedetomidine postconditioning.
    Bcl2 Adenovirus E1b 19 Kda Interacting Protein 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher bcl2 adenovirus e1b 19kda interacting protein 3
    Western blots of BNIP3, BNIP3 L, HIF-1α and LC3II. BNIP3, <t>Bcl-2/adenovirus</t> E1B <t>19-kDa</t> interacting protein 3; BNIP3 L, BNIP3 like; HIF-1α, hypoxia-inducible factor 1α; LC3II, microtubule-associated protein 1A/1B light chain 3B; IR, ischemia-reperfusion; pre-LD, low-dose dexmedetomidine preconditioning; pre-HD, high-dose dexmedetomidine preconditioning; post-LD, low-dose dexmedetomidine postconditioning; post-HD, high-dose dexmedetomidine postconditioning.
    Bcl2 Adenovirus E1b 19kda Interacting Protein 3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega adenovirus e1b tata sequence pg5luc
    Western blots of BNIP3, BNIP3 L, HIF-1α and LC3II. BNIP3, <t>Bcl-2/adenovirus</t> E1B <t>19-kDa</t> interacting protein 3; BNIP3 L, BNIP3 like; HIF-1α, hypoxia-inducible factor 1α; LC3II, microtubule-associated protein 1A/1B light chain 3B; IR, ischemia-reperfusion; pre-LD, low-dose dexmedetomidine preconditioning; pre-HD, high-dose dexmedetomidine preconditioning; post-LD, low-dose dexmedetomidine postconditioning; post-HD, high-dose dexmedetomidine postconditioning.
    Adenovirus E1b Tata Sequence Pg5luc, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Oncogene Science Inc e1b 19 kda
    HCMV IE1 and IE2 genes and their products are not present in transformed BRK cell lines. ( A ) Lack of expression of the IE1 or IE2 protein in transformed BRK cell lines when assayed by immunoprecipitation of 35 S-labeled cell extracts using monoclonal antibody mAB810. A-1 is a cell line established by transfection with the E1A-expressing plasmid alone. A/1/2–1 to A/1/2–10 are cell lines transformed by E1A plus IE1 and IE2. Lanes designated HCMV INF display immunoprecipitates from HCMV-infected human foreskin fibroblasts; lane 13 is an exposure 1/8 as long as that presented for lanes 1–12. Numbers to the left of the gel mark the positions of marker proteins whose sizes are indicated in <t>kDa.</t> ( B ) Southern blot analysis showing the lack of IE1 - or IE2 -specific DNA in E1A/IE1/IE2-induced transformants (lanes 1–10). A/B-1 and A/B-2 are cell lines transformed with E1A and <t>E1B-19-kDa.</t> HeLa, 293, and HP1.14 (a derivative HeLa cells expressing IE1) are included as controls. pCGN-IE1 and pCGN-IE2 are IE1 and IE2 expression plasmids, respectively, in amounts equivalent to the rest of the samples, assuming they contain one copy of each of the HCMV genes per cell. Numbers to the left of the gel are marker DNA sizes in kb. ( C ) Expression of E1A protein as determined by immunoprecipitation followed by immunoblot analysis, both with monoclonal antibody M73 to E1A. Lanes are labeled as in A and B . Numbers to the left of the gel are marker protein sizes in kDa. Autoradiograms were scanned and cropped using Photoshop and figures were prepared using Freehand software.
    E1b 19 Kda, supplied by Oncogene Science Inc, used in various techniques. Bioz Stars score: 80/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Oncogene Science Inc e1b 19k rat mab
    HCMV IE1 and IE2 genes and their products are not present in transformed BRK cell lines. ( A ) Lack of expression of the IE1 or IE2 protein in transformed BRK cell lines when assayed by immunoprecipitation of 35 S-labeled cell extracts using monoclonal antibody mAB810. A-1 is a cell line established by transfection with the E1A-expressing plasmid alone. A/1/2–1 to A/1/2–10 are cell lines transformed by E1A plus IE1 and IE2. Lanes designated HCMV INF display immunoprecipitates from HCMV-infected human foreskin fibroblasts; lane 13 is an exposure 1/8 as long as that presented for lanes 1–12. Numbers to the left of the gel mark the positions of marker proteins whose sizes are indicated in <t>kDa.</t> ( B ) Southern blot analysis showing the lack of IE1 - or IE2 -specific DNA in E1A/IE1/IE2-induced transformants (lanes 1–10). A/B-1 and A/B-2 are cell lines transformed with E1A and <t>E1B-19-kDa.</t> HeLa, 293, and HP1.14 (a derivative HeLa cells expressing IE1) are included as controls. pCGN-IE1 and pCGN-IE2 are IE1 and IE2 expression plasmids, respectively, in amounts equivalent to the rest of the samples, assuming they contain one copy of each of the HCMV genes per cell. Numbers to the left of the gel are marker DNA sizes in kb. ( C ) Expression of E1A protein as determined by immunoprecipitation followed by immunoblot analysis, both with monoclonal antibody M73 to E1A. Lanes are labeled as in A and B . Numbers to the left of the gel are marker protein sizes in kDa. Autoradiograms were scanned and cropped using Photoshop and figures were prepared using Freehand software.
    E1b 19k Rat Mab, supplied by Oncogene Science Inc, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    becton dickinson e1b 19k
    HCMV IE1 and IE2 genes and their products are not present in transformed BRK cell lines. ( A ) Lack of expression of the IE1 or IE2 protein in transformed BRK cell lines when assayed by immunoprecipitation of 35 S-labeled cell extracts using monoclonal antibody mAB810. A-1 is a cell line established by transfection with the E1A-expressing plasmid alone. A/1/2–1 to A/1/2–10 are cell lines transformed by E1A plus IE1 and IE2. Lanes designated HCMV INF display immunoprecipitates from HCMV-infected human foreskin fibroblasts; lane 13 is an exposure 1/8 as long as that presented for lanes 1–12. Numbers to the left of the gel mark the positions of marker proteins whose sizes are indicated in <t>kDa.</t> ( B ) Southern blot analysis showing the lack of IE1 - or IE2 -specific DNA in E1A/IE1/IE2-induced transformants (lanes 1–10). A/B-1 and A/B-2 are cell lines transformed with E1A and <t>E1B-19-kDa.</t> HeLa, 293, and HP1.14 (a derivative HeLa cells expressing IE1) are included as controls. pCGN-IE1 and pCGN-IE2 are IE1 and IE2 expression plasmids, respectively, in amounts equivalent to the rest of the samples, assuming they contain one copy of each of the HCMV genes per cell. Numbers to the left of the gel are marker DNA sizes in kb. ( C ) Expression of E1A protein as determined by immunoprecipitation followed by immunoblot analysis, both with monoclonal antibody M73 to E1A. Lanes are labeled as in A and B . Numbers to the left of the gel are marker protein sizes in kDa. Autoradiograms were scanned and cropped using Photoshop and figures were prepared using Freehand software.
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    Genewiz e1b 55 kda insert
    Viral DNA synthesis is inhibited in AdEasyE1Sub19-infected cells treated with IFN. (A) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19) for the periods indicated or mock infected (M). The proteins listed at the right were examined by immunoblotting of total cell lysates as described in Materials and Methods. (B) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]) or AdEasyE1Sub19 (S19) for 36 h or mock infected (mock), and the E1B <t>55-kDa</t> protein was visualized by immunofluorescence as described in Materials and Methods. DAPI, 4′,6-diamidino-2-phenylindole. (C) HFFs were treated with IFN or untreated (BSA) and infected with 3 PFU/cell of the virus indicated for 2 or 72 h. Viral DNA concentrations were measured by quantitative PCR, with cellular β-actin DNA used as an internal control, as described in Materials and Methods, and are expressed relative to the input (2 h) concentrations. The values represent the averages of two independent experiments, with cumulative standard deviations indicated by the error bars.
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    OriGene e1b 55 k ap 000199 expression vectors
    Viral DNA synthesis is inhibited in AdEasyE1Sub19-infected cells treated with IFN. (A) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19) for the periods indicated or mock infected (M). The proteins listed at the right were examined by immunoblotting of total cell lysates as described in Materials and Methods. (B) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]) or AdEasyE1Sub19 (S19) for 36 h or mock infected (mock), and the E1B <t>55-kDa</t> protein was visualized by immunofluorescence as described in Materials and Methods. DAPI, 4′,6-diamidino-2-phenylindole. (C) HFFs were treated with IFN or untreated (BSA) and infected with 3 PFU/cell of the virus indicated for 2 or 72 h. Viral DNA concentrations were measured by quantitative PCR, with cellular β-actin DNA used as an internal control, as described in Materials and Methods, and are expressed relative to the input (2 h) concentrations. The values represent the averages of two independent experiments, with cumulative standard deviations indicated by the error bars.
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    Image Search Results


    Clusters of coregulated cellular RNAs 30 h after infection with Ad5 or E1B mutants. The expression profiles of significantly regulated genes were clustered into eight distinct groups with similar expression response profiles across the different Ad5 genotypes as described in Materials and Methods. Each cluster was searched for statistically significant enrichment of genes that code for proteins with common functions ( P values are Bonferroni corrected for multiple hypothesis testing). GO terms enriched in clusters 2, 3, and 4 are shown at right, with the corresponding P values. Genes that increased and decreased in expression are shown in yellow and blue, respectively, as indicated on the scale bar. hpi, hours postinfection.

    Journal: Journal of Virology

    Article Title: The Adenoviral E1B 55-Kilodalton Protein Controls Expression of Immune Response Genes but Not p53-Dependent Transcription ▿

    doi: 10.1128/JVI.02269-08

    Figure Lengend Snippet: Clusters of coregulated cellular RNAs 30 h after infection with Ad5 or E1B mutants. The expression profiles of significantly regulated genes were clustered into eight distinct groups with similar expression response profiles across the different Ad5 genotypes as described in Materials and Methods. Each cluster was searched for statistically significant enrichment of genes that code for proteins with common functions ( P values are Bonferroni corrected for multiple hypothesis testing). GO terms enriched in clusters 2, 3, and 4 are shown at right, with the corresponding P values. Genes that increased and decreased in expression are shown in yellow and blue, respectively, as indicated on the scale bar. hpi, hours postinfection.

    Article Snippet: Plasmids carrying the desired mutations were identified by the presence of a new restriction endonuclease site, and the presence of the mutations was confirmed by sequencing the E1B gene (Genewiz Inc.).

    Techniques: Infection, Expressing

    Effects of the sub17 mutations on accumulation of the E1B 55-kDa protein and protein V. (A) The coding sequences of the E1B proteins are shown to scale below the arrow representing the major E1B mRNA species, with different reading frames in white, gray, and black. As summarized above the mRNA, deletion of bp 2437 in the Hr6 genomes results in a shift of reading frame and termination of translation a short distance downstream. The C-terminal sequences of the wild-type and sub17 E1B 55-kDa proteins are shown between the expansion lines below, with the substitutions indicated in bold. (B) The E1B 55-kDa protein was examined 36 h after infection with Ad5 or Ad5E1B-sub17 (S17) or in mock-infected cells (M) by immunoblotting as described in Materials and Methods. Numbers at left are molecular masses in kilodaltons.

    Journal: Journal of Virology

    Article Title: The Adenoviral E1B 55-Kilodalton Protein Controls Expression of Immune Response Genes but Not p53-Dependent Transcription ▿

    doi: 10.1128/JVI.02269-08

    Figure Lengend Snippet: Effects of the sub17 mutations on accumulation of the E1B 55-kDa protein and protein V. (A) The coding sequences of the E1B proteins are shown to scale below the arrow representing the major E1B mRNA species, with different reading frames in white, gray, and black. As summarized above the mRNA, deletion of bp 2437 in the Hr6 genomes results in a shift of reading frame and termination of translation a short distance downstream. The C-terminal sequences of the wild-type and sub17 E1B 55-kDa proteins are shown between the expansion lines below, with the substitutions indicated in bold. (B) The E1B 55-kDa protein was examined 36 h after infection with Ad5 or Ad5E1B-sub17 (S17) or in mock-infected cells (M) by immunoblotting as described in Materials and Methods. Numbers at left are molecular masses in kilodaltons.

    Article Snippet: Plasmids carrying the desired mutations were identified by the presence of a new restriction endonuclease site, and the presence of the mutations was confirmed by sequencing the E1B gene (Genewiz Inc.).

    Techniques: Infection

    Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × UAS:smoa1-EGFP) and the Tg(UAS-E1b:nfsB-mCherry) c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).

    Journal: Oncogenesis

    Article Title: Activation of Sonic hedgehog signaling in neural progenitor cells promotes glioma development in the zebrafish optic pathway

    doi: 10.1038/oncsis.2014.10

    Figure Lengend Snippet: Phenotypic characterization of a stable transgenic line. ( a ) Graphic representation of the DNA constructs used for transgenesis and breeding. ( b ) A 24 h.p.f. embryo expresses Smoa1-EGFP in the forebrain and retinal neuroblasts. A 96 h.p.f. double transgenic embryo derived from crossing of the Tg(krt5:Gal4VP16;14 × UAS:smoa1-EGFP) and the Tg(UAS-E1b:nfsB-mCherry) c264 stable lines expressed GFP ( c ) and mCherry ( d ) in the ONs (arrows). ( e ) A 6-month-old wild-type and ( f ) a transgenic fish with a gross tumor in its left eye (arrow). ( g ) Wild-type fish formed a normal optic chiasm, whereas ( h ) transgenic fish failed to form optic chiasm and showed dramatic expansion of the ONH region (arrow). ( i ) Dissected brain and eyes showing an enlarged ON associating with a gross eye tumor (arrow).

    Article Snippet: Zebrafish husbandry AB and Tg(UAS-E1b:nfsB-mCherry) c264 strains were acquired from the Zebrafish International Resource Center (ZIRC, Eugene, OR, USA).

    Techniques: Transgenic Assay, Construct, Derivative Assay, Fluorescence In Situ Hybridization

    KSHV ORF57 interacts with PABPC1. (A) ORF57 interacts with PABPC1, but not with E1B-AP5, as shown by coimmunoprecipitation assays. Total cell extracts from TREx BCBL1-Rta cells induced by Dox (1 μg/ml) and treated with a mixture of RNase A and T1 were immunoprecipitated with preimmune mouse IgG- or monoclonal anti-ORF57 antibody-coated beads and examined for PABPC1 and E1B-AP5 by Western blotting (left). Conversely, the same extracts treated with a mixture of RNase A and T1 were immunoprecipitated with nonspecific rabbit IgG- or polyclonal anti-PABPC1 or anti-E1B-AP5 antibody-coated beads and blotted for ORF57 by Western blotting (right). (B) PABPC1 directly interacts with ORF57, as shown by GST pulldown assays. Full-length PABPC1 protein with an N-terminal GST tag or untagged GST was immobilized on glutathione-Sepharose 4B beads and incubated at 4°C overnight in IP buffer complemented with KSHV ORF57 protein containing a C-terminal FLAG tag that was expressed from baculovirus. The glutathione-Sepharose 4B beads without any GST protein were used as an additional negative control. After binding, the beads were washed five times with IP buffer, resuspended in 2× SDS sample buffer, and analyzed by Western blotting with two antibodies, an anti-GST antibody recognizing PABPC1 and an anti-FLAG antibody that recognizes the epitope-tagged ORF57.

    Journal: Journal of Virology

    Article Title: Interplay between Polyadenylate-Binding Protein 1 and Kaposi's Sarcoma-Associated Herpesvirus ORF57 in Accumulation of Polyadenylated Nuclear RNA, a Viral Long Noncoding RNA

    doi: 10.1128/JVI.01693-12

    Figure Lengend Snippet: KSHV ORF57 interacts with PABPC1. (A) ORF57 interacts with PABPC1, but not with E1B-AP5, as shown by coimmunoprecipitation assays. Total cell extracts from TREx BCBL1-Rta cells induced by Dox (1 μg/ml) and treated with a mixture of RNase A and T1 were immunoprecipitated with preimmune mouse IgG- or monoclonal anti-ORF57 antibody-coated beads and examined for PABPC1 and E1B-AP5 by Western blotting (left). Conversely, the same extracts treated with a mixture of RNase A and T1 were immunoprecipitated with nonspecific rabbit IgG- or polyclonal anti-PABPC1 or anti-E1B-AP5 antibody-coated beads and blotted for ORF57 by Western blotting (right). (B) PABPC1 directly interacts with ORF57, as shown by GST pulldown assays. Full-length PABPC1 protein with an N-terminal GST tag or untagged GST was immobilized on glutathione-Sepharose 4B beads and incubated at 4°C overnight in IP buffer complemented with KSHV ORF57 protein containing a C-terminal FLAG tag that was expressed from baculovirus. The glutathione-Sepharose 4B beads without any GST protein were used as an additional negative control. After binding, the beads were washed five times with IP buffer, resuspended in 2× SDS sample buffer, and analyzed by Western blotting with two antibodies, an anti-GST antibody recognizing PABPC1 and an anti-FLAG antibody that recognizes the epitope-tagged ORF57.

    Article Snippet: Rabbit anti-PABPC1 antibody (ab21060; Abcam) and anti-E1B-AP5 antibody (ab68480; Abcam) were used for IP.

    Techniques: Immunoprecipitation, Western Blot, Incubation, FLAG-tag, Negative Control, Binding Assay

    ). This model proposes that the PAN MRE-II-mediated interactions and cross-talks between 5′ capping and 3′ polyadenylation machineries via ORF57, PABPC1, and E1B-AP5 maximize PAN stability.

    Journal: Journal of Virology

    Article Title: Interplay between Polyadenylate-Binding Protein 1 and Kaposi's Sarcoma-Associated Herpesvirus ORF57 in Accumulation of Polyadenylated Nuclear RNA, a Viral Long Noncoding RNA

    doi: 10.1128/JVI.01693-12

    Figure Lengend Snippet: ). This model proposes that the PAN MRE-II-mediated interactions and cross-talks between 5′ capping and 3′ polyadenylation machineries via ORF57, PABPC1, and E1B-AP5 maximize PAN stability.

    Article Snippet: Rabbit anti-PABPC1 antibody (ab21060; Abcam) and anti-E1B-AP5 antibody (ab68480; Abcam) were used for IP.

    Techniques:

    KSHV lytic infection induces host gene shutoff and nuclear distribution of cytoplasmic PABPC1. (A) Pie chart summary of PABPC1 status in ORF57-expressing BCBL1 cells after KSHV lytic induction. TREx BCBL1-Rta cells induced with Dox for 48 h were fixed and double stained with anti-PABPC1 and anti-ORF57 antibodies and imaged by confocal microscopy. A total of 282 cells, with or without PABPC1 and ORF57, were randomly counted in multiple microscope image fields, and only 209 cells with ORF57 staining were calculated for PABPC1 status. (B) Reduction of PABPC1 and β-tubulin in BCBL1 cells with lytic KSHV induction. Total protein was prepared from BCBL1 cells 48 h after lytic KSHV infection induced by 1 mM VA and host gene expression of PABPC1 and β-tubulin, and the presence of ORF57 was examined by Western blotting. BCBL1 cells without lytic induction (uninduced [unind.]) served as a control. (C and D) ORF57-expressing B cells undergoing lytic KSHV infection exhibit redistribution of PABPC1 but not E1B-AP5. TREx BCBL1-vector (a to d) or TREx BCBL1-Rta (e to h) cells induced by Dox were stained with either rabbit anti-PABPC1 (C) or E1B-AP5 (D) antibodies along with a mouse monoclonal anti-ORF57 antibody. Confocal imaging was performed as described in Materials and Methods. The nuclear distributions of cytoplasmic PABPC1 (red) (C) and nuclear E1B-AP5 (red) (D) were seen in ORF57-positive (green) TREx BCBL1-Rta cells. DAPI, 4′,6′-diamino-2-phenylindole nuclear staining.

    Journal: Journal of Virology

    Article Title: Interplay between Polyadenylate-Binding Protein 1 and Kaposi's Sarcoma-Associated Herpesvirus ORF57 in Accumulation of Polyadenylated Nuclear RNA, a Viral Long Noncoding RNA

    doi: 10.1128/JVI.01693-12

    Figure Lengend Snippet: KSHV lytic infection induces host gene shutoff and nuclear distribution of cytoplasmic PABPC1. (A) Pie chart summary of PABPC1 status in ORF57-expressing BCBL1 cells after KSHV lytic induction. TREx BCBL1-Rta cells induced with Dox for 48 h were fixed and double stained with anti-PABPC1 and anti-ORF57 antibodies and imaged by confocal microscopy. A total of 282 cells, with or without PABPC1 and ORF57, were randomly counted in multiple microscope image fields, and only 209 cells with ORF57 staining were calculated for PABPC1 status. (B) Reduction of PABPC1 and β-tubulin in BCBL1 cells with lytic KSHV induction. Total protein was prepared from BCBL1 cells 48 h after lytic KSHV infection induced by 1 mM VA and host gene expression of PABPC1 and β-tubulin, and the presence of ORF57 was examined by Western blotting. BCBL1 cells without lytic induction (uninduced [unind.]) served as a control. (C and D) ORF57-expressing B cells undergoing lytic KSHV infection exhibit redistribution of PABPC1 but not E1B-AP5. TREx BCBL1-vector (a to d) or TREx BCBL1-Rta (e to h) cells induced by Dox were stained with either rabbit anti-PABPC1 (C) or E1B-AP5 (D) antibodies along with a mouse monoclonal anti-ORF57 antibody. Confocal imaging was performed as described in Materials and Methods. The nuclear distributions of cytoplasmic PABPC1 (red) (C) and nuclear E1B-AP5 (red) (D) were seen in ORF57-positive (green) TREx BCBL1-Rta cells. DAPI, 4′,6′-diamino-2-phenylindole nuclear staining.

    Article Snippet: Rabbit anti-PABPC1 antibody (ab21060; Abcam) and anti-E1B-AP5 antibody (ab68480; Abcam) were used for IP.

    Techniques: Infection, Expressing, Staining, Confocal Microscopy, Microscopy, Western Blot, Plasmid Preparation, Imaging

    Roles of PABPC1 and E1B-AP5 in PAN expression. (A) Endogenous PABPC1 is inhibitory for PAN expression. PABPC1 in HeLa cells was knocked down using a PABPC1-specific siRNA (siPABPC1) in the presence or absence of ORF57. A nonspecific siRNA (siControl) was employed as a control. The PABPC1-knockdown efficiency was analyzed by Western blotting (WB). Total RNA of HeLa cells transfected with siPABPC1 or siControl, together with PAN-expressing vector pJM1 in the presence (+) or absence (−) of ORF57, was examined by Northern blotting (NB) with a 32 ) were transfected twice, at intervals of 24 h, with 40 nM PABPC1-specific siRNA or a nonspecific control siRNA before viral lytic induction by either 3 mM butyrate for 24 h (Bu 24) or 1 mM valproate for 48 h (VA 48). The cells were harvested after virus induction for total protein and RNA preparation. The efficiency of PABPC1 knockdown was examined by Western blotting of total protein, and β-tubulin served as a loading control. PAN RNA was determined by Northern blotting of 3 μg of total RNA for Bac36-wt cells and 5 μg of total RNA for Bac36-Δ57 cells using the 32 P-labeled, PAN-specific oligonucleotide probe oJM7. GAPDH RNA in panels A to C served as a sample loading control. The relative levels (signal intensity) of PAN RNA in each sample in panel C were calculated after normalization to the level of GAPDH RNA. A relative ratio (fold) of PAN in siPABPC1- to siControl-treated cells in panels A to C was determined according to the normalized levels in each sample pair.

    Journal: Journal of Virology

    Article Title: Interplay between Polyadenylate-Binding Protein 1 and Kaposi's Sarcoma-Associated Herpesvirus ORF57 in Accumulation of Polyadenylated Nuclear RNA, a Viral Long Noncoding RNA

    doi: 10.1128/JVI.01693-12

    Figure Lengend Snippet: Roles of PABPC1 and E1B-AP5 in PAN expression. (A) Endogenous PABPC1 is inhibitory for PAN expression. PABPC1 in HeLa cells was knocked down using a PABPC1-specific siRNA (siPABPC1) in the presence or absence of ORF57. A nonspecific siRNA (siControl) was employed as a control. The PABPC1-knockdown efficiency was analyzed by Western blotting (WB). Total RNA of HeLa cells transfected with siPABPC1 or siControl, together with PAN-expressing vector pJM1 in the presence (+) or absence (−) of ORF57, was examined by Northern blotting (NB) with a 32 ) were transfected twice, at intervals of 24 h, with 40 nM PABPC1-specific siRNA or a nonspecific control siRNA before viral lytic induction by either 3 mM butyrate for 24 h (Bu 24) or 1 mM valproate for 48 h (VA 48). The cells were harvested after virus induction for total protein and RNA preparation. The efficiency of PABPC1 knockdown was examined by Western blotting of total protein, and β-tubulin served as a loading control. PAN RNA was determined by Northern blotting of 3 μg of total RNA for Bac36-wt cells and 5 μg of total RNA for Bac36-Δ57 cells using the 32 P-labeled, PAN-specific oligonucleotide probe oJM7. GAPDH RNA in panels A to C served as a sample loading control. The relative levels (signal intensity) of PAN RNA in each sample in panel C were calculated after normalization to the level of GAPDH RNA. A relative ratio (fold) of PAN in siPABPC1- to siControl-treated cells in panels A to C was determined according to the normalized levels in each sample pair.

    Article Snippet: Rabbit anti-PABPC1 antibody (ab21060; Abcam) and anti-E1B-AP5 antibody (ab68480; Abcam) were used for IP.

    Techniques: Expressing, Western Blot, Transfection, Plasmid Preparation, Northern Blot, Labeling

    Identification of nuclear transport factor 2 (NTF2)-like export protein 1 (NXT1) as a binding partner of influenza nucleoprotein (NP). ( A ) NP-FLAG or FLAG- non-structural 1 (NS1) protein was immobilized on anti-FLAG agarose beads and co-incubated with HeLa whole cell lysate overnight at 4 °C. The beads were collected, washed, and subjected to western blot (WB) analysis with anti-NXT1, anti-NUP153, anti-NUP98, anti-NUP62, anti-E1B-AP5, anti-CRM1, or anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials. Black arrowheads indicate specific binding. H and L indicate the heavy and light chains of the agarose-conjugated anti-FLAG antibody; ( B ) Human embryonic kidney (HEK293T) cells were transfected with NP-FLAG/pCAGGS and HA-NXT1/pCAGGS plasmids for 48 h, lysed, and incubated with anti-FLAG agarose beads overnight at 4 °C. The agarose beads were collected, washed, and subjected to WB analysis with anti- hemagglutinin (HA) and anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials; ( C ) HA-NXT1 protein was immobilized on anti-HA agarose beads and co-incubated with purified NP-FLAG protein overnight at 4 °C. The beads were collected, washed, and subjected to WB analysis with anti-FLAG and anti-HA antibodies. Data shown are the results of one representative experiment from three independent trials.

    Journal: Viruses

    Article Title: NXT1, a Novel Influenza A NP Binding Protein, Promotes the Nuclear Export of NP via a CRM1-Dependent Pathway

    doi: 10.3390/v8080209

    Figure Lengend Snippet: Identification of nuclear transport factor 2 (NTF2)-like export protein 1 (NXT1) as a binding partner of influenza nucleoprotein (NP). ( A ) NP-FLAG or FLAG- non-structural 1 (NS1) protein was immobilized on anti-FLAG agarose beads and co-incubated with HeLa whole cell lysate overnight at 4 °C. The beads were collected, washed, and subjected to western blot (WB) analysis with anti-NXT1, anti-NUP153, anti-NUP98, anti-NUP62, anti-E1B-AP5, anti-CRM1, or anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials. Black arrowheads indicate specific binding. H and L indicate the heavy and light chains of the agarose-conjugated anti-FLAG antibody; ( B ) Human embryonic kidney (HEK293T) cells were transfected with NP-FLAG/pCAGGS and HA-NXT1/pCAGGS plasmids for 48 h, lysed, and incubated with anti-FLAG agarose beads overnight at 4 °C. The agarose beads were collected, washed, and subjected to WB analysis with anti- hemagglutinin (HA) and anti-FLAG antibodies. Data shown are the results of one representative experiment from two independent trials; ( C ) HA-NXT1 protein was immobilized on anti-HA agarose beads and co-incubated with purified NP-FLAG protein overnight at 4 °C. The beads were collected, washed, and subjected to WB analysis with anti-FLAG and anti-HA antibodies. Data shown are the results of one representative experiment from three independent trials.

    Article Snippet: Antibodies used for analysis were anti-NXT1 rabbit polyclonal antibody (pAb) (Abnova, Taipei, Taiwan), anti-CRM1 mouse monoclonal antibody (mAb) (BD Biosciences, San Jose, CA, USA), anti-NUP153 rat mAb (Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-NUP98 rat mAb (Abcam, Cambridge, UK), anti-NUP62 mouse mAb (BD Biosciences), anti-E1B-AP5 (or hnRNP UL1) mouse mAb (Santa Cruz Biotechnology), anti-FLAG M2 mouse mAb (Sigma-Aldrich, Saint Louis, MO, USA), anti-FLAG rabbit mAb (Sigma-Aldrich), anti-HA mouse mAb (Medical and Biological Laboratories, Nagoya, Japan), anti-β-actin mouse mAb (Sigma-Aldrich), anti-WSN (influenza A/WSN/33) rabbit pAb (a gift from Dr. Kazufumi Shimizu, Nihon University School of Medicine, Tokyo, Japan), horseradish-peroxidase (HRP)-conjugated goat anti-mouse IgG (Amersham Biosciences, Uppsala, Sweden), or HRP-conjugated goat anti-rabbit IgG (Amersham Biosciences).

    Techniques: Binding Assay, Incubation, Western Blot, Transfection, Purification

    Western blots of BNIP3, BNIP3 L, HIF-1α and LC3II. BNIP3, Bcl-2/adenovirus E1B 19-kDa interacting protein 3; BNIP3 L, BNIP3 like; HIF-1α, hypoxia-inducible factor 1α; LC3II, microtubule-associated protein 1A/1B light chain 3B; IR, ischemia-reperfusion; pre-LD, low-dose dexmedetomidine preconditioning; pre-HD, high-dose dexmedetomidine preconditioning; post-LD, low-dose dexmedetomidine postconditioning; post-HD, high-dose dexmedetomidine postconditioning.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Dexmedetomidine preconditioning protects against lung injury induced by ischemia-reperfusion through inhibition of autophagy

    doi: 10.3892/etm.2017.4623

    Figure Lengend Snippet: Western blots of BNIP3, BNIP3 L, HIF-1α and LC3II. BNIP3, Bcl-2/adenovirus E1B 19-kDa interacting protein 3; BNIP3 L, BNIP3 like; HIF-1α, hypoxia-inducible factor 1α; LC3II, microtubule-associated protein 1A/1B light chain 3B; IR, ischemia-reperfusion; pre-LD, low-dose dexmedetomidine preconditioning; pre-HD, high-dose dexmedetomidine preconditioning; post-LD, low-dose dexmedetomidine postconditioning; post-HD, high-dose dexmedetomidine postconditioning.

    Article Snippet: The membranes were blocked with 5% skimmed milk in Tris-buffered saline with Tween 20 for 1 h at room temperature, and then incubated overnight at 4°C with rabbit polyclonal antibodies directed against hypoxia-inducible factor 1α (HIF-1α; cat no. sc13515; 1:1,000; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), Bcl-2/adenovirus E1B 19-kDa interacting protein 3 (BNIP3; cat no. sc56167; 1:1,000; Santa Cruz Biotechnology, Inc.), BNIP3-like (BNIP3L; cat no. ab109414; 1:1,000; Abcam, Cambridge, USA) and microtubule-associated protein 1A/1B light chain 3B (LC3II; cat no. sc271625; 1:1,000; Santa Cruz Biotechnology Inc.).

    Techniques: Western Blot

    HCMV IE1 and IE2 genes and their products are not present in transformed BRK cell lines. ( A ) Lack of expression of the IE1 or IE2 protein in transformed BRK cell lines when assayed by immunoprecipitation of 35 S-labeled cell extracts using monoclonal antibody mAB810. A-1 is a cell line established by transfection with the E1A-expressing plasmid alone. A/1/2–1 to A/1/2–10 are cell lines transformed by E1A plus IE1 and IE2. Lanes designated HCMV INF display immunoprecipitates from HCMV-infected human foreskin fibroblasts; lane 13 is an exposure 1/8 as long as that presented for lanes 1–12. Numbers to the left of the gel mark the positions of marker proteins whose sizes are indicated in kDa. ( B ) Southern blot analysis showing the lack of IE1 - or IE2 -specific DNA in E1A/IE1/IE2-induced transformants (lanes 1–10). A/B-1 and A/B-2 are cell lines transformed with E1A and E1B-19-kDa. HeLa, 293, and HP1.14 (a derivative HeLa cells expressing IE1) are included as controls. pCGN-IE1 and pCGN-IE2 are IE1 and IE2 expression plasmids, respectively, in amounts equivalent to the rest of the samples, assuming they contain one copy of each of the HCMV genes per cell. Numbers to the left of the gel are marker DNA sizes in kb. ( C ) Expression of E1A protein as determined by immunoprecipitation followed by immunoblot analysis, both with monoclonal antibody M73 to E1A. Lanes are labeled as in A and B . Numbers to the left of the gel are marker protein sizes in kDa. Autoradiograms were scanned and cropped using Photoshop and figures were prepared using Freehand software.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Human cytomegalovirus IE1 and IE2 proteins are mutagenic and mediate "hit-and-run" oncogenic transformation in cooperation with the adenovirus E1A proteins

    doi:

    Figure Lengend Snippet: HCMV IE1 and IE2 genes and their products are not present in transformed BRK cell lines. ( A ) Lack of expression of the IE1 or IE2 protein in transformed BRK cell lines when assayed by immunoprecipitation of 35 S-labeled cell extracts using monoclonal antibody mAB810. A-1 is a cell line established by transfection with the E1A-expressing plasmid alone. A/1/2–1 to A/1/2–10 are cell lines transformed by E1A plus IE1 and IE2. Lanes designated HCMV INF display immunoprecipitates from HCMV-infected human foreskin fibroblasts; lane 13 is an exposure 1/8 as long as that presented for lanes 1–12. Numbers to the left of the gel mark the positions of marker proteins whose sizes are indicated in kDa. ( B ) Southern blot analysis showing the lack of IE1 - or IE2 -specific DNA in E1A/IE1/IE2-induced transformants (lanes 1–10). A/B-1 and A/B-2 are cell lines transformed with E1A and E1B-19-kDa. HeLa, 293, and HP1.14 (a derivative HeLa cells expressing IE1) are included as controls. pCGN-IE1 and pCGN-IE2 are IE1 and IE2 expression plasmids, respectively, in amounts equivalent to the rest of the samples, assuming they contain one copy of each of the HCMV genes per cell. Numbers to the left of the gel are marker DNA sizes in kb. ( C ) Expression of E1A protein as determined by immunoprecipitation followed by immunoblot analysis, both with monoclonal antibody M73 to E1A. Lanes are labeled as in A and B . Numbers to the left of the gel are marker protein sizes in kDa. Autoradiograms were scanned and cropped using Photoshop and figures were prepared using Freehand software.

    Article Snippet: For the two sets of coverslips collected from cells transfected with vectors expressing the E1A plus E1B-19-kDa proteins, one set was stained with anti-E1A antibody (M73), and the other was stained with monoclonal antibody to E1B-19-kDa (Oncogene Science).

    Techniques: Transformation Assay, Expressing, Immunoprecipitation, Labeling, Transfection, Plasmid Preparation, Infection, Marker, Southern Blot, Software

    The IE1 and IE2 gene products are expressed transiently during the transformation of BRK cells. BRK cells seeded on coverslips were transfected with expression plasmids for E1A and E1B-19-kDa ( Left ) or plasmids for E1A and IE1 and IE2 ( Right ). At 2, 5, 13, and 19 days after transfection, two coverslips from each transfection were fixed and kept in phosphate-buffered saline until coverslips for all time points were collected. Expression of the transfected genes was examined by indirect immunofluorescent staining with appropriate monoclonal antibodies. Anti-E1A, anti-E1B-19-kDa, and anti-IE1/2 identify the antibodies used for the immunofluorescent staining. Images are from independent coverslips. The images from days 13 and 19 display transformed foci whose cells were positive for E1A and E1B-19-kDa proteins, but completely negative for IE1 and IE2 protein expression. (×50).

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Human cytomegalovirus IE1 and IE2 proteins are mutagenic and mediate "hit-and-run" oncogenic transformation in cooperation with the adenovirus E1A proteins

    doi:

    Figure Lengend Snippet: The IE1 and IE2 gene products are expressed transiently during the transformation of BRK cells. BRK cells seeded on coverslips were transfected with expression plasmids for E1A and E1B-19-kDa ( Left ) or plasmids for E1A and IE1 and IE2 ( Right ). At 2, 5, 13, and 19 days after transfection, two coverslips from each transfection were fixed and kept in phosphate-buffered saline until coverslips for all time points were collected. Expression of the transfected genes was examined by indirect immunofluorescent staining with appropriate monoclonal antibodies. Anti-E1A, anti-E1B-19-kDa, and anti-IE1/2 identify the antibodies used for the immunofluorescent staining. Images are from independent coverslips. The images from days 13 and 19 display transformed foci whose cells were positive for E1A and E1B-19-kDa proteins, but completely negative for IE1 and IE2 protein expression. (×50).

    Article Snippet: For the two sets of coverslips collected from cells transfected with vectors expressing the E1A plus E1B-19-kDa proteins, one set was stained with anti-E1A antibody (M73), and the other was stained with monoclonal antibody to E1B-19-kDa (Oncogene Science).

    Techniques: Transformation Assay, Transfection, Expressing, Staining

    Viral DNA synthesis is inhibited in AdEasyE1Sub19-infected cells treated with IFN. (A) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19) for the periods indicated or mock infected (M). The proteins listed at the right were examined by immunoblotting of total cell lysates as described in Materials and Methods. (B) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]) or AdEasyE1Sub19 (S19) for 36 h or mock infected (mock), and the E1B 55-kDa protein was visualized by immunofluorescence as described in Materials and Methods. DAPI, 4′,6-diamidino-2-phenylindole. (C) HFFs were treated with IFN or untreated (BSA) and infected with 3 PFU/cell of the virus indicated for 2 or 72 h. Viral DNA concentrations were measured by quantitative PCR, with cellular β-actin DNA used as an internal control, as described in Materials and Methods, and are expressed relative to the input (2 h) concentrations. The values represent the averages of two independent experiments, with cumulative standard deviations indicated by the error bars.

    Journal: Journal of Virology

    Article Title: The Repression Domain of the E1B 55-Kilodalton Protein Participates in Countering Interferon-Induced Inhibition of Adenovirus Replication

    doi: 10.1128/JVI.03387-12

    Figure Lengend Snippet: Viral DNA synthesis is inhibited in AdEasyE1Sub19-infected cells treated with IFN. (A) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19) for the periods indicated or mock infected (M). The proteins listed at the right were examined by immunoblotting of total cell lysates as described in Materials and Methods. (B) HFFs were infected with 30 PFU/cell AdEasyE1 (wild type [WT]) or AdEasyE1Sub19 (S19) for 36 h or mock infected (mock), and the E1B 55-kDa protein was visualized by immunofluorescence as described in Materials and Methods. DAPI, 4′,6-diamidino-2-phenylindole. (C) HFFs were treated with IFN or untreated (BSA) and infected with 3 PFU/cell of the virus indicated for 2 or 72 h. Viral DNA concentrations were measured by quantitative PCR, with cellular β-actin DNA used as an internal control, as described in Materials and Methods, and are expressed relative to the input (2 h) concentrations. The values represent the averages of two independent experiments, with cumulative standard deviations indicated by the error bars.

    Article Snippet: The sequence of the E1B 55-kDa insert was verified by sequencing (Genewiz).

    Techniques: DNA Synthesis, Infection, Immunofluorescence, Real-time Polymerase Chain Reaction

    Effects of the E1B 55-kDa Sub19 alterations on activation of Stat1. Mock-infected HFFs were treated with 250 units/ml IFN or vehicle-only control (BSA) for 24 h. Cells were infected with 200 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19) for the periods indicated, and the proteins listed at the right were examined by immunoblotting of whole-cell lysates as described in Materials and Methods. Stat1 phosphorylated on Tyr701 is designated Stat1-P.

    Journal: Journal of Virology

    Article Title: The Repression Domain of the E1B 55-Kilodalton Protein Participates in Countering Interferon-Induced Inhibition of Adenovirus Replication

    doi: 10.1128/JVI.03387-12

    Figure Lengend Snippet: Effects of the E1B 55-kDa Sub19 alterations on activation of Stat1. Mock-infected HFFs were treated with 250 units/ml IFN or vehicle-only control (BSA) for 24 h. Cells were infected with 200 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19) for the periods indicated, and the proteins listed at the right were examined by immunoblotting of whole-cell lysates as described in Materials and Methods. Stat1 phosphorylated on Tyr701 is designated Stat1-P.

    Article Snippet: The sequence of the E1B 55-kDa insert was verified by sequencing (Genewiz).

    Techniques: Activation Assay, Infection

    The Sub19 substitutions impair repression of expression of IFN-inducible genes by the E1B 55-kDa protein. HFFs untreated (BSA) or treated with IFN (IFN) were infected with 200 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19), and total cell RNA was isolated 47 h after infection. The concentrations of GBP1 (A) and IFIT2 (B) mRNAs were determined by quantitative PCR, after synthesis of cDNA by reverse transcription from random primers, as described in Materials and Methods. The values shown represent the averages and cumulative standard deviations (bars) of two independent experiments.

    Journal: Journal of Virology

    Article Title: The Repression Domain of the E1B 55-Kilodalton Protein Participates in Countering Interferon-Induced Inhibition of Adenovirus Replication

    doi: 10.1128/JVI.03387-12

    Figure Lengend Snippet: The Sub19 substitutions impair repression of expression of IFN-inducible genes by the E1B 55-kDa protein. HFFs untreated (BSA) or treated with IFN (IFN) were infected with 200 PFU/cell AdEasyE1 (wild type [WT]), AdEasyE1Δ2347 (ΔE1B), or AdEasyE1Sub19 (S19), and total cell RNA was isolated 47 h after infection. The concentrations of GBP1 (A) and IFIT2 (B) mRNAs were determined by quantitative PCR, after synthesis of cDNA by reverse transcription from random primers, as described in Materials and Methods. The values shown represent the averages and cumulative standard deviations (bars) of two independent experiments.

    Article Snippet: The sequence of the E1B 55-kDa insert was verified by sequencing (Genewiz).

    Techniques: Expressing, Infection, Isolation, Real-time Polymerase Chain Reaction