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  • 99
    New England Biolabs messenger rna mrna magnetic isolation module
    The KH domains of IGF2BPs are critical for m 6 A recognition and binding ( a ) Schematic structures showing <t>RNA</t> binding domains within IGF2BP proteins and a summary of IGF2BP variants used in this study. Blue boxes are RRM domains, red boxes are wild-type KH domains with GxxG core, and grey boxes are inactive KH domain with GxxG to GEEG conversions. ( b ) RNA pulldown followed by Western blotting showed in vitro binding of ssRNA baits with wild-type (wt) or KH domain-mutated IGF2BP variants, representative of 3 independent experiments. ( c ) In vitro binding of CRD1 RNA probes with wild-type or KH3-4 mutated IGF2BPs, representative of 3 independent experiments. ( d ) The association of wild-type and KH3-4 mutated IGF2BPs with MYC CRD in HEK293T cells as assessed by RIP-qPCR. ( e ) Relative luciferase activity of CRD reporters in HEK293T cells with forced expression of wild-type or mutated IGF2BP2 variants. ( f ) Changes in MYC <t>mRNA</t> levels in Hela cells with empty vector or forced expression of wild-type or KH3-4 mutated IGF2BPs one hour post-heat shock (HS). Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in d , e , f (*, P
    Messenger Rna Mrna Magnetic Isolation Module, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1085 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/messenger rna mrna magnetic isolation module/product/New England Biolabs
    Average 99 stars, based on 1085 article reviews
    Price from $9.99 to $1999.99
    messenger rna mrna magnetic isolation module - by Bioz Stars, 2020-07
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    90
    Illumina Inc mrna magnetic isolation module
    The KH domains of IGF2BPs are critical for m 6 A recognition and binding ( a ) Schematic structures showing <t>RNA</t> binding domains within IGF2BP proteins and a summary of IGF2BP variants used in this study. Blue boxes are RRM domains, red boxes are wild-type KH domains with GxxG core, and grey boxes are inactive KH domain with GxxG to GEEG conversions. ( b ) RNA pulldown followed by Western blotting showed in vitro binding of ssRNA baits with wild-type (wt) or KH domain-mutated IGF2BP variants, representative of 3 independent experiments. ( c ) In vitro binding of CRD1 RNA probes with wild-type or KH3-4 mutated IGF2BPs, representative of 3 independent experiments. ( d ) The association of wild-type and KH3-4 mutated IGF2BPs with MYC CRD in HEK293T cells as assessed by RIP-qPCR. ( e ) Relative luciferase activity of CRD reporters in HEK293T cells with forced expression of wild-type or mutated IGF2BP2 variants. ( f ) Changes in MYC <t>mRNA</t> levels in Hela cells with empty vector or forced expression of wild-type or KH3-4 mutated IGF2BPs one hour post-heat shock (HS). Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in d , e , f (*, P
    Mrna Magnetic Isolation Module, supplied by Illumina Inc, used in various techniques. Bioz Stars score: 90/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mrna magnetic isolation module/product/Illumina Inc
    Average 90 stars, based on 33 article reviews
    Price from $9.99 to $1999.99
    mrna magnetic isolation module - by Bioz Stars, 2020-07
    90/100 stars
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    93
    Thermo Fisher mrna magnetic isolation module
    The KH domains of IGF2BPs are critical for m 6 A recognition and binding ( a ) Schematic structures showing <t>RNA</t> binding domains within IGF2BP proteins and a summary of IGF2BP variants used in this study. Blue boxes are RRM domains, red boxes are wild-type KH domains with GxxG core, and grey boxes are inactive KH domain with GxxG to GEEG conversions. ( b ) RNA pulldown followed by Western blotting showed in vitro binding of ssRNA baits with wild-type (wt) or KH domain-mutated IGF2BP variants, representative of 3 independent experiments. ( c ) In vitro binding of CRD1 RNA probes with wild-type or KH3-4 mutated IGF2BPs, representative of 3 independent experiments. ( d ) The association of wild-type and KH3-4 mutated IGF2BPs with MYC CRD in HEK293T cells as assessed by RIP-qPCR. ( e ) Relative luciferase activity of CRD reporters in HEK293T cells with forced expression of wild-type or mutated IGF2BP2 variants. ( f ) Changes in MYC <t>mRNA</t> levels in Hela cells with empty vector or forced expression of wild-type or KH3-4 mutated IGF2BPs one hour post-heat shock (HS). Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in d , e , f (*, P
    Mrna Magnetic Isolation Module, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mrna magnetic isolation module/product/Thermo Fisher
    Average 93 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    mrna magnetic isolation module - by Bioz Stars, 2020-07
    93/100 stars
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    99
    New England Biolabs mrna magnetic isolation module kit
    The KH domains of IGF2BPs are critical for m 6 A recognition and binding ( a ) Schematic structures showing <t>RNA</t> binding domains within IGF2BP proteins and a summary of IGF2BP variants used in this study. Blue boxes are RRM domains, red boxes are wild-type KH domains with GxxG core, and grey boxes are inactive KH domain with GxxG to GEEG conversions. ( b ) RNA pulldown followed by Western blotting showed in vitro binding of ssRNA baits with wild-type (wt) or KH domain-mutated IGF2BP variants, representative of 3 independent experiments. ( c ) In vitro binding of CRD1 RNA probes with wild-type or KH3-4 mutated IGF2BPs, representative of 3 independent experiments. ( d ) The association of wild-type and KH3-4 mutated IGF2BPs with MYC CRD in HEK293T cells as assessed by RIP-qPCR. ( e ) Relative luciferase activity of CRD reporters in HEK293T cells with forced expression of wild-type or mutated IGF2BP2 variants. ( f ) Changes in MYC <t>mRNA</t> levels in Hela cells with empty vector or forced expression of wild-type or KH3-4 mutated IGF2BPs one hour post-heat shock (HS). Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in d , e , f (*, P
    Mrna Magnetic Isolation Module Kit, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mrna magnetic isolation module kit/product/New England Biolabs
    Average 99 stars, based on 35 article reviews
    Price from $9.99 to $1999.99
    mrna magnetic isolation module kit - by Bioz Stars, 2020-07
    99/100 stars
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    Image Search Results


    The KH domains of IGF2BPs are critical for m 6 A recognition and binding ( a ) Schematic structures showing RNA binding domains within IGF2BP proteins and a summary of IGF2BP variants used in this study. Blue boxes are RRM domains, red boxes are wild-type KH domains with GxxG core, and grey boxes are inactive KH domain with GxxG to GEEG conversions. ( b ) RNA pulldown followed by Western blotting showed in vitro binding of ssRNA baits with wild-type (wt) or KH domain-mutated IGF2BP variants, representative of 3 independent experiments. ( c ) In vitro binding of CRD1 RNA probes with wild-type or KH3-4 mutated IGF2BPs, representative of 3 independent experiments. ( d ) The association of wild-type and KH3-4 mutated IGF2BPs with MYC CRD in HEK293T cells as assessed by RIP-qPCR. ( e ) Relative luciferase activity of CRD reporters in HEK293T cells with forced expression of wild-type or mutated IGF2BP2 variants. ( f ) Changes in MYC mRNA levels in Hela cells with empty vector or forced expression of wild-type or KH3-4 mutated IGF2BPs one hour post-heat shock (HS). Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in d , e , f (*, P

    Journal: Nature cell biology

    Article Title: Recognition of RNA N6-methyladenosine by IGF2BP Proteins Enhances mRNA Stability and Translation

    doi: 10.1038/s41556-018-0045-z

    Figure Lengend Snippet: The KH domains of IGF2BPs are critical for m 6 A recognition and binding ( a ) Schematic structures showing RNA binding domains within IGF2BP proteins and a summary of IGF2BP variants used in this study. Blue boxes are RRM domains, red boxes are wild-type KH domains with GxxG core, and grey boxes are inactive KH domain with GxxG to GEEG conversions. ( b ) RNA pulldown followed by Western blotting showed in vitro binding of ssRNA baits with wild-type (wt) or KH domain-mutated IGF2BP variants, representative of 3 independent experiments. ( c ) In vitro binding of CRD1 RNA probes with wild-type or KH3-4 mutated IGF2BPs, representative of 3 independent experiments. ( d ) The association of wild-type and KH3-4 mutated IGF2BPs with MYC CRD in HEK293T cells as assessed by RIP-qPCR. ( e ) Relative luciferase activity of CRD reporters in HEK293T cells with forced expression of wild-type or mutated IGF2BP2 variants. ( f ) Changes in MYC mRNA levels in Hela cells with empty vector or forced expression of wild-type or KH3-4 mutated IGF2BPs one hour post-heat shock (HS). Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in d , e , f (*, P

    Article Snippet: PolyA RNA was subsequently purified from 50–100 ng total RNA using NEBNext Poly(A) mRNA Magnetic Isolation Module.

    Techniques: Binding Assay, RNA Binding Assay, Western Blot, In Vitro, Real-time Polymerase Chain Reaction, Luciferase, Activity Assay, Expressing, Plasmid Preparation, Two Tailed Test

    IGF2BPs regulate MYC expression through binding to methylated CRD ( a ) Distribution of m 6 A peaks across MYC mRNA transcript. The coding region instability determinant (CRD) region is highlighted in yellow. m 6 A-seq was repeated twice while RIP-seq was performed once.( b ) RIP-qPCR showing the association of MYC CRD with FLAG-tagged IGF2BPs in HEK293T cells. ( c ) Enrichment of m 6 A modification in MYC CRD as detected by gene specific m 6 A qPCR assay. ( d ) RIP-qPCR showing the binding of METTL3 and METTL14 to the MYC CRD. ( e ) RNA pulldown of endogenous IGF2BP proteins from HEK293T nuclear extract using synthetic CRD RNA fragments, CRD1 and CRD2, with (m 6 A) or without (A) m 6 A modifications. Images are representative of 3 independent experiments. ( f ) Relative firefly luciferase (Fluc) activity (i.e., protein level; left) and Fluc mRNA level (right) of wild-type (CRD-wt) or mutated (CRD-mut) CRD reporters in HEK293T cells with ectopically expressed IGF2BP1, IGF2BP2, or IGF2BP3. ( g ) RIP-qPCR detecting the in vivo binding of Flag-IGF2BPs to the transcripts of CRD-wt or CRD-mut luciferase reporter in HEK293T cells. ( h and i ) Relative luciferase activity of CRD-wt or CRD-mut in Hela cells with or without stable knockdown of IGF2BPs (h) or METTL14 (i). ( j ) Relative luciferase activity of CRD-wt or CRD-mut in METTL14 stable knockdown or control Hela cells with ectopic expression of IGF2BPs . For all luciferase assays, the Fluc/Rluc ratio (representing luciferase activity) of CRD-wt with empty vector or shNS was used for normalization. Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in b , c , d , f , g , h , i , j . (**, P

    Journal: Nature cell biology

    Article Title: Recognition of RNA N6-methyladenosine by IGF2BP Proteins Enhances mRNA Stability and Translation

    doi: 10.1038/s41556-018-0045-z

    Figure Lengend Snippet: IGF2BPs regulate MYC expression through binding to methylated CRD ( a ) Distribution of m 6 A peaks across MYC mRNA transcript. The coding region instability determinant (CRD) region is highlighted in yellow. m 6 A-seq was repeated twice while RIP-seq was performed once.( b ) RIP-qPCR showing the association of MYC CRD with FLAG-tagged IGF2BPs in HEK293T cells. ( c ) Enrichment of m 6 A modification in MYC CRD as detected by gene specific m 6 A qPCR assay. ( d ) RIP-qPCR showing the binding of METTL3 and METTL14 to the MYC CRD. ( e ) RNA pulldown of endogenous IGF2BP proteins from HEK293T nuclear extract using synthetic CRD RNA fragments, CRD1 and CRD2, with (m 6 A) or without (A) m 6 A modifications. Images are representative of 3 independent experiments. ( f ) Relative firefly luciferase (Fluc) activity (i.e., protein level; left) and Fluc mRNA level (right) of wild-type (CRD-wt) or mutated (CRD-mut) CRD reporters in HEK293T cells with ectopically expressed IGF2BP1, IGF2BP2, or IGF2BP3. ( g ) RIP-qPCR detecting the in vivo binding of Flag-IGF2BPs to the transcripts of CRD-wt or CRD-mut luciferase reporter in HEK293T cells. ( h and i ) Relative luciferase activity of CRD-wt or CRD-mut in Hela cells with or without stable knockdown of IGF2BPs (h) or METTL14 (i). ( j ) Relative luciferase activity of CRD-wt or CRD-mut in METTL14 stable knockdown or control Hela cells with ectopic expression of IGF2BPs . For all luciferase assays, the Fluc/Rluc ratio (representing luciferase activity) of CRD-wt with empty vector or shNS was used for normalization. Values are mean±s.d. of n =3 independent experiments, and two-tailed Student’s t -tests were used in b , c , d , f , g , h , i , j . (**, P

    Article Snippet: PolyA RNA was subsequently purified from 50–100 ng total RNA using NEBNext Poly(A) mRNA Magnetic Isolation Module.

    Techniques: Expressing, Binding Assay, Methylation, Real-time Polymerase Chain Reaction, Modification, Luciferase, Activity Assay, In Vivo, Plasmid Preparation, Two Tailed Test

    Selective binding of IGF2BPs to m 6 A-modified RNAs ( a ) Identification of m 6 A specific binding proteins by RNA affinity chromatography using ssRNA probes with methylated (red) or unmethylated (green) adenosine. Silver staining (lower left) and Western blotting (lower right) showed selective pulldown of ~68kDa IGF2BP proteins from HEK293T nuclear extract. Western blot images were representative of 3 independent experiments. ( b ) Enrichment of m 6 A consensus sequence “GGAC” in the binding sites of RBPs. The three IGF2BP paralogues were shown in red, while the YTH domain proteins were shown in orange. ( c ) Quantification of m 6 A/A and m 6 A/AGCU ratios by LC-MS/MS in RNAs bound by ectopically expressed IGF2BP1 (chicken ZBP1), IGF2BP2 (human), or IGF2BP3 (human). Values are mean of n =2 independent experiments and individual data points are showed. ( d ) Overlap of IGF2BP target genes identified by RIP-seq and published PAR-CLIP in HEK293T cells. RIP-seq was performed once. P value was calculated by Fisher’s test. ( e ) Venn diagram showing the numbers of shared high-confidence targets ( i.e. , CLIP+RIP targets) amongst IGF2BP paralogues. P value was calculated by Fisher’s test. ( f ) Top consensus sequences of IGF2BP binding sites and the m 6 A motif detected by HOMER Motif analysis with PAR-CLIP data. ( g ) Pie charts showing numbers and percentages of IGF2BP high-confidence target genes that contain m 6 A peaks. The m 6 A-seq data was reported in Ref. 3 . ( h ) Metagene profiles of enrichment of IGF2BP binding sites and m 6 A modifications across mRNA transcriptome. ( i ) Percentages of various RNA species bound by IGF2BPs. ( j ) The distribution (upper) and enrichment (lower) of IGF2BPs binding peaks within different gene reions. The enrichment was determined by the proportion of IGF2BPs binding peaks normalized by the length of the region. Analyses in i and j were performed twice with similar results. ( k ) In vivo binding of Flag-IGF2BP2 to representative target genes in METTL14 knockdown or control HEK293T cells. Values are mean±s.d. of n =3 independent experiments. *, P

    Journal: Nature cell biology

    Article Title: Recognition of RNA N6-methyladenosine by IGF2BP Proteins Enhances mRNA Stability and Translation

    doi: 10.1038/s41556-018-0045-z

    Figure Lengend Snippet: Selective binding of IGF2BPs to m 6 A-modified RNAs ( a ) Identification of m 6 A specific binding proteins by RNA affinity chromatography using ssRNA probes with methylated (red) or unmethylated (green) adenosine. Silver staining (lower left) and Western blotting (lower right) showed selective pulldown of ~68kDa IGF2BP proteins from HEK293T nuclear extract. Western blot images were representative of 3 independent experiments. ( b ) Enrichment of m 6 A consensus sequence “GGAC” in the binding sites of RBPs. The three IGF2BP paralogues were shown in red, while the YTH domain proteins were shown in orange. ( c ) Quantification of m 6 A/A and m 6 A/AGCU ratios by LC-MS/MS in RNAs bound by ectopically expressed IGF2BP1 (chicken ZBP1), IGF2BP2 (human), or IGF2BP3 (human). Values are mean of n =2 independent experiments and individual data points are showed. ( d ) Overlap of IGF2BP target genes identified by RIP-seq and published PAR-CLIP in HEK293T cells. RIP-seq was performed once. P value was calculated by Fisher’s test. ( e ) Venn diagram showing the numbers of shared high-confidence targets ( i.e. , CLIP+RIP targets) amongst IGF2BP paralogues. P value was calculated by Fisher’s test. ( f ) Top consensus sequences of IGF2BP binding sites and the m 6 A motif detected by HOMER Motif analysis with PAR-CLIP data. ( g ) Pie charts showing numbers and percentages of IGF2BP high-confidence target genes that contain m 6 A peaks. The m 6 A-seq data was reported in Ref. 3 . ( h ) Metagene profiles of enrichment of IGF2BP binding sites and m 6 A modifications across mRNA transcriptome. ( i ) Percentages of various RNA species bound by IGF2BPs. ( j ) The distribution (upper) and enrichment (lower) of IGF2BPs binding peaks within different gene reions. The enrichment was determined by the proportion of IGF2BPs binding peaks normalized by the length of the region. Analyses in i and j were performed twice with similar results. ( k ) In vivo binding of Flag-IGF2BP2 to representative target genes in METTL14 knockdown or control HEK293T cells. Values are mean±s.d. of n =3 independent experiments. *, P

    Article Snippet: PolyA RNA was subsequently purified from 50–100 ng total RNA using NEBNext Poly(A) mRNA Magnetic Isolation Module.

    Techniques: Binding Assay, Modification, Affinity Chromatography, Methylation, Silver Staining, Western Blot, Sequencing, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Cross-linking Immunoprecipitation, In Vivo

    Electropherograms from five embryos of soybean seeds harvested in 1994 (stored 23 years, orange dashed lines) or 2015 (stored 2 years, green solid lines). (A) Total RNA from each sample. The differences in peak heights in 1994H relative to 2015H samples indicate RNA degradation. (B) DNAse-treated, poly-A RNA. The most abundant mRNAs are smaller in 1994H seeds than 2015H seeds.

    Journal: Journal of Experimental Botany

    Article Title: Exploring the fate of mRNA in aging seeds: protection, destruction, or slow decay?

    doi: 10.1093/jxb/ery215

    Figure Lengend Snippet: Electropherograms from five embryos of soybean seeds harvested in 1994 (stored 23 years, orange dashed lines) or 2015 (stored 2 years, green solid lines). (A) Total RNA from each sample. The differences in peak heights in 1994H relative to 2015H samples indicate RNA degradation. (B) DNAse-treated, poly-A RNA. The most abundant mRNAs are smaller in 1994H seeds than 2015H seeds.

    Article Snippet: The NEBNext Poly(A) mRNA Magnetic Isolation Module (New England Biolabs, Ipswich, MA, USA) was used to enrich for mRNA according to the manufacturer’s protocol.

    Techniques: