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    Thermo Fisher rnase inhibitor rnaseout
    Eudicot <t>S-RNase</t> protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and <t>5′RACE</t> data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .
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    Promega rnaseout recombinant rnase inhibitor
    Eudicot <t>S-RNase</t> protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and <t>5′RACE</t> data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .
    Rnaseout Recombinant Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rnase out rnase inhibitor
    Eudicot <t>S-RNase</t> protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and <t>5′RACE</t> data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .
    Rnase Out Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 918 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega rnase inhibitor
    Eudicot <t>S-RNase</t> protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and <t>5′RACE</t> data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .
    Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 10015 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rnase a inhibitor rnaseout
    Eudicot <t>S-RNase</t> protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and <t>5′RACE</t> data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .
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    Image Search Results


    Eudicot S-RNase protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and 5′RACE data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .

    Journal: PLoS ONE

    Article Title: Expression and Trans-Specific Polymorphism of Self-Incompatibility RNases in Coffea (Rubiaceae)

    doi: 10.1371/journal.pone.0021019

    Figure Lengend Snippet: Eudicot S-RNase protein conserved domain structure. The conserved domain structures of S-RNases employed in GSI Eudicot lineages and the conserved domains revealed in this study of Coffea are labeled accordingly. Canonical S-RNase conserved regions are labeled “c1”–“c5”, and hyper-variable regions are labeled “HVa” and “HVb”. The red arrowheads below the protein constructs indicate intron positions. Intron position data and presence of conserved region c1 was validated in Coffea based on genomic sequence and 5′RACE data from C. arabica and C. canephora alone (data not shown). Results relating to RNase polymorphism reported in this study are based on 3′RACE data from the hyper-variable regions (i.e. HVa) to the end of transcripts (i.e. through c5). This figure was adapted from Vieira and Charlesworth [91] .

    Article Snippet: Briefly, first strand cDNA was synthesized from heat-denatured (80°C for 5 mins) total RNA (150 ng – 1 µg) with MMLV reverse transcriptase (Promega), RNase inhibitor (RNaseOut, Invitrogen), and a 3′ RACE adapter primer at 37°C for one hour.

    Techniques: Labeling, Construct, Sequencing

    Expression of RNase T2 genes in C. arabica tissues. Agarose gel image showing RT-PCR results using gene-specific primers for Coffea RNase “A”, “C”, and S-RNase genes. cDNAs were generated from RNA extracts of various C. arabica tissues labeled as follows: P1 = pre-anthesis pistils dissected from flower buds; P2 = post-anthesis pistils; L1 = leaf at 1 week; L2 = leaf at > 2 weeks; R1 = fine root; R2 = primary root; F1 = fruit at approximately 1 week; F2 = fruit at > 3 weeks. RNase “A” and “C” genes are constitutively expressed in C. arabica tissues, but the S-RNase gene shows pistil-specific expression characteristic of genes involved in the S-RNase GSI system.

    Journal: PLoS ONE

    Article Title: Expression and Trans-Specific Polymorphism of Self-Incompatibility RNases in Coffea (Rubiaceae)

    doi: 10.1371/journal.pone.0021019

    Figure Lengend Snippet: Expression of RNase T2 genes in C. arabica tissues. Agarose gel image showing RT-PCR results using gene-specific primers for Coffea RNase “A”, “C”, and S-RNase genes. cDNAs were generated from RNA extracts of various C. arabica tissues labeled as follows: P1 = pre-anthesis pistils dissected from flower buds; P2 = post-anthesis pistils; L1 = leaf at 1 week; L2 = leaf at > 2 weeks; R1 = fine root; R2 = primary root; F1 = fruit at approximately 1 week; F2 = fruit at > 3 weeks. RNase “A” and “C” genes are constitutively expressed in C. arabica tissues, but the S-RNase gene shows pistil-specific expression characteristic of genes involved in the S-RNase GSI system.

    Article Snippet: Briefly, first strand cDNA was synthesized from heat-denatured (80°C for 5 mins) total RNA (150 ng – 1 µg) with MMLV reverse transcriptase (Promega), RNase inhibitor (RNaseOut, Invitrogen), and a 3′ RACE adapter primer at 37°C for one hour.

    Techniques: Expressing, Agarose Gel Electrophoresis, Reverse Transcription Polymerase Chain Reaction, Generated, Labeling

    Interactions between PIWI proteins and histone modification-related proteins. ( A ) Co-immunoprecipitation (Co-IP) assay of PIWIL1 and WDR5 by anti-HA agarose beads followed by immunoblots with indicated antibodies (middle). ( B ) Co-IP assay of PIWIL4 and WDR5. ( C ) Co-IP assay of PIWIL1 and PIWIL4. ( D ) Co-IP assay of PIWIL1 and WDR5 after RNase treatment by anti-HA agarose beads followed by immunoblots. ( E ) Co-IP assay of PIWIL1 and WDR5 in the presence or absence of MLL3 or UTX by anti-HA antibodies followed by immunoblots. ( F ) Co-IP assay of PIWIL1 and MLL3 in the presence or absence of WDR5 or UTX. ( G ) Co-IP assay of PIWIL1 and UTX in the presence or absence of WDR5 or MLL3. ( H ) Endogenous co-IP assay of PIWIL1 and WDR5 in MCF7 cells by using anti-PIWIL1 antibody. ( I ) association of WDR5 with the TRAIL promoter under the overexpression of pi-sno75 was detected by ChIP-qPCR. The relative enrichment was calculated by normalizing the quantity of TRAIL DNA against the quantity of input. ( J ) The association of PIWIL1 with the TRAIL promoter in the absence of WDR5 was detected by ChIP-qPCR. ( K ) The association of WDR5 with the TRAIL promoter in the absence of PIWIL1 was detected by ChIP-qPCR. Bar graphs represent mean ± SD ( n = 3). *, statistically significant, ≤0.05.

    Journal: Nucleic Acids Research

    Article Title: An Lnc RNA (GAS5)/SnoRNA-derived piRNA induces activation of TRAIL gene by site-specifically recruiting MLL/COMPASS-like complexes

    doi: 10.1093/nar/gkv214

    Figure Lengend Snippet: Interactions between PIWI proteins and histone modification-related proteins. ( A ) Co-immunoprecipitation (Co-IP) assay of PIWIL1 and WDR5 by anti-HA agarose beads followed by immunoblots with indicated antibodies (middle). ( B ) Co-IP assay of PIWIL4 and WDR5. ( C ) Co-IP assay of PIWIL1 and PIWIL4. ( D ) Co-IP assay of PIWIL1 and WDR5 after RNase treatment by anti-HA agarose beads followed by immunoblots. ( E ) Co-IP assay of PIWIL1 and WDR5 in the presence or absence of MLL3 or UTX by anti-HA antibodies followed by immunoblots. ( F ) Co-IP assay of PIWIL1 and MLL3 in the presence or absence of WDR5 or UTX. ( G ) Co-IP assay of PIWIL1 and UTX in the presence or absence of WDR5 or MLL3. ( H ) Endogenous co-IP assay of PIWIL1 and WDR5 in MCF7 cells by using anti-PIWIL1 antibody. ( I ) association of WDR5 with the TRAIL promoter under the overexpression of pi-sno75 was detected by ChIP-qPCR. The relative enrichment was calculated by normalizing the quantity of TRAIL DNA against the quantity of input. ( J ) The association of PIWIL1 with the TRAIL promoter in the absence of WDR5 was detected by ChIP-qPCR. ( K ) The association of WDR5 with the TRAIL promoter in the absence of PIWIL1 was detected by ChIP-qPCR. Bar graphs represent mean ± SD ( n = 3). *, statistically significant, ≤0.05.

    Article Snippet: RNA immunoprecipitation To detect whether the small RNAs were associated with the PIWI proteins, PBMCs were homogenized using immunoprecipitation (IP) lysis buffer plus RNase inhibitor RNaseOUT (40 units/ml, Invitrogen).

    Techniques: Modification, Co-Immunoprecipitation Assay, Western Blot, Over Expression, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction