shrna kd chip seq data (Novogene)
86
Structured Review
Novogene
shrna kd chip seq data
Shrna Kd Chip Seq Data, supplied by Novogene, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chip+seq+data/chip+library+preparation+seq/pmc12901234-338-2-8
Average 86 stars, based on 1 article reviews
Shrna Kd Chip Seq Data, supplied by Novogene, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chip+seq+data/chip+library+preparation+seq/pmc12901234-338-2-8
Average 86 stars, based on 1 article reviews
shrna kd chip seq data - by Bioz Stars,
2026-09
86/100 stars
Images
1) Product Images from "EPOP restricts PRC2.1 targeting to chromatin by directly modulating enzyme complex dimerization"
Article Title: EPOP restricts PRC2.1 targeting to chromatin by directly modulating enzyme complex dimerization
Journal: Nature Communications
doi: 10.1038/s41467-025-68280-5
Figure Legend Snippet: a Re-expression of WT and mutant EPOP in mESCs. Representative of two biological replicates . b Co-IP assay of re-expressed EPOP. The re-expressed 3 × FLAG-EPOP-HA protein was used as the bait, and the bound endogenous SUZ12 was detected. Representative of two replicates. c Schematic of the EpiLC differentiation. Some parts of the figure were created in BioRender. Liu, X. (2026) ( https://biorender.com/gvraoqv ). d Heatmaps of ChIP-seq replicates. Using the FDR < 0.05 threshold, the gain-of-signal MTF2 (purple) and H3K27me3 (green) peaks from individual replicates (WT-1, WT-2, D5-1, and D5-2) are shown in the heatmaps. The centers of the consensus binding sites are aligned. The number of the consensus binding sites is labeled. e Metaplots of ChIP-seq replicates. The mean ChIP-seq signal of the differential MTF2 (upper panel) and H3K27me3 (lower panel) peaks shown in ( d ) is plotted. The individual replicates are color-coded. f Genome browser tracks of selected gene loci. Tracks were generated by SparK ( https://github.com/harbourlab/SparK ). Genomic coordinates are provided. The difference between the replicates, calculated as the standard deviation, is indicated as the shaded areas surrounding the tracks. g Scatter plots of MTF2 and H3K27me3. MTF2 (left panel) and H3K27me3 (right panel) reads were normalized by the total reads. The mean read concentration corresponding to log2 (normalized ChIP-seq reads with input reads subtracted) was calculated by DiffBind.
Techniques Used: Expressing, Mutagenesis, Co-Immunoprecipitation Assay, ChIP-sequencing, Binding Assay, Labeling, Generated, Standard Deviation, Concentration Assay
Figure Legend Snippet: a Heatmaps of ChIP-seq replicates. The differential MTF2 peaks between the EPOP WT and EPOP D5 EpiLCs were grouped into three categories based on the response to shRNA KD, using the FDR < 0.05 threshold. Differential peaks shared by the control and Elongin B KD are labeled as n1, differential peaks unique to the control KD are labeled as n2, and differential peaks unique to the Elongin B KD are labeled as n3. b Genome browser tracks of selected gene loci. Tracks were generated by SparK. Two gene loci associated with the shared differential MTF2 peaks between the control KD and the Elongin B KD are shown. c Venn diagram of the differential MTF2 peaks in the three categories.
Techniques Used: ChIP-sequencing, shRNA, Control, Labeling, Generated
Figure Legend Snippet: a Volcano plot of differential gene expression. RNA-seq results of the EPOP D5 EpiLCs in triplicates were compared to those of the EPOP WT EpiLCs. The number of upregulated and downregulated genes is indicated. Data passing the FDR < 0.05, FC > 1.5, and average TPM of WT or mutant > 0.5 thresholds were analyzed. b Correlation of RNA-seq and ChIP-seq. One ChIP-seq replicate is shown here, and the other replicate is shown in the supplemental materials. The differential gene expression was aligned with the differential MTF2 enrichment around the transcription start site (TSS). The corresponding H3K27me3 signals are also displayed. Compared to the WT counterpart, 130 genes in the EPOP D5 EpiLCs were downregulated and associated with enhanced MTF2 signals around the TSS. The other 318 downregulated genes were not associated with EPOP-regulated MTF2 targeting. 187 upregulated genes are shown as well. c Gene ontology analysis. The PRC2.1-repressed, EPOP-maintained genes were subjected to gene ontology analysis on the DAVID server. The top 5 overrepresented terms in molecular function are shown. The p -value is one-tail Fisher Exact probability value used for gene-enrichment analysis by the DAVID server. d Schematic model of developmental gene repression by PRC2. On the left, the transient intrinsic dimer of the PRC2 core complex is illustrated. In the middle, distinct oligomerization states of various PRC2.1 and PRC2.2 holocomplexes are highlighted. MTF2 mediates direct chromatin binding, and it also stabilizes the intrinsic dimer, promoting chromatin targeting of the dimeric PRC2.1, likely via an avidity effect. EPOP disrupts the dimeric architecture of PRC2.1, containing MTF2, restricts PRC2.1 targeting, and thereby maintains the limited expression of PRC2.1-repressed developmental regulators. On the right, the PRC2.1-dependent role of EPOP in early development is illustrated. Black solid curve: during the ESC differentiation, a set of key gene regulators is repressed by PRC2.1, with limited expression being maintained by the EPOP-mediated inhibition of PRC2.1 targeting, which is followed by upregulation of the same set of gene regulators, leading to cell fate 1, e.g., PGCLCs. Gray dotted curve: the absence of EPOP results in the over-repression of these gene regulators by PRC2.1, which may change stem cell differentiation trajectories and result in an alternative cell fate 2. Some parts of the figure were created in BioRender. Liu, X. (2026) ( https://biorender.com/l3ji249 ).
Techniques Used: Gene Expression, RNA Sequencing, Mutagenesis, ChIP-sequencing, Binding Assay, Expressing, Inhibition, Cell Differentiation
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Immunoprecipitated DNA was subjected to Polymerase Chain Reaction:Article Title: Modulation of rob expression accelerates development of antibiotic resistance in Yersinia enterocolitica Article Snippet: Followed by transcription initiation blocking with rifampicin (final 150 mg/L; stock 50 mg/mL in methanol, 300 μL per sample) for 20 min at 28 °C, 220 rpm; cells were crosslinked by adding 37% formaldehyde to 1% final for 20 min at 28 °C, 220 rpm, and the reaction was quenched by adding 2.5 M glycine to 125 mM final, incubating 20 min at 4 °C with gentle shaking; cells were pelleted (6000×g, 5 min, 25 °C), washed three times with 1× PBS, and pellets were processed immediately or stored at −80 °C; pellets were resuspended in 200 μL lysozyme (20 mg/mL) and incubated 30 min at 37 °C, chromatin was fragmented by sonication (Covaris, M220 Focused-ultra-sonicator) for 3 minutes to generate DNA fragments of approximately 150–400 bp, debris were removed (14,000 rpm, 10 min); lysates were pre-cleared with 50 μL Protein A/G beads (MedChemExpress) for 2 h at 4 °C on a rotating wheel, beads were pelleted (13,800×g, 1 min) and the supernatant was incubated with 10 μL mouse anti-FLAG antibody overnight at 4 °C with rotation, then immune complexes were captured with 50 μL Protein A/G beads for 6 h at 4 °C (or overnight) and beads were collected (10,000 rpm, 5 min), washed four times with lysis buffer (NaCl, HEPES, sodium deoxycholate, Triton X-100, DTT, protease inhibitor cocktail 1:100, and Tris-HCl) at 4 °C (1 mL each; 14,000 rpm, 5 min) and twice with TE buffer; complexes were eluted with 100 μL elution buffer 1 at 65 °C for 10 min and then 150 μL elution buffer 2, pooling eluates (250 μL total), and crosslinks were reversed at 65 °C for 6 h or overnight; 10% eluate (25 μL) was reserved for optional Western blot, the remainder was treated with RNase A (20 μL; 100 mg/L) for 30 min at 37 °C and digested with proteinase K (250 μL of a proteinase K/glycogen mix prepared in TE) for 2 h at 58 °C, followed by DNA cleanup with 4 M LiCl (55 μL), phenol:chloroform:isoamyl alcohol extraction (25:24:1) and ethanol precipitation (−80 °C, 30 min; 14,000 rpm, 5 min, 4 °C), washing with 70% ethanol, air-drying, and resuspension in 25 μL nuclease-free water; DNA was quantified (Qubit) and stored at −20 °C. .. Immunoprecipitated DNA was subjected to Amplification:Article Title: Modulation of rob expression accelerates development of antibiotic resistance in Yersinia enterocolitica Article Snippet: Followed by transcription initiation blocking with rifampicin (final 150 mg/L; stock 50 mg/mL in methanol, 300 μL per sample) for 20 min at 28 °C, 220 rpm; cells were crosslinked by adding 37% formaldehyde to 1% final for 20 min at 28 °C, 220 rpm, and the reaction was quenched by adding 2.5 M glycine to 125 mM final, incubating 20 min at 4 °C with gentle shaking; cells were pelleted (6000×g, 5 min, 25 °C), washed three times with 1× PBS, and pellets were processed immediately or stored at −80 °C; pellets were resuspended in 200 μL lysozyme (20 mg/mL) and incubated 30 min at 37 °C, chromatin was fragmented by sonication (Covaris, M220 Focused-ultra-sonicator) for 3 minutes to generate DNA fragments of approximately 150–400 bp, debris were removed (14,000 rpm, 10 min); lysates were pre-cleared with 50 μL Protein A/G beads (MedChemExpress) for 2 h at 4 °C on a rotating wheel, beads were pelleted (13,800×g, 1 min) and the supernatant was incubated with 10 μL mouse anti-FLAG antibody overnight at 4 °C with rotation, then immune complexes were captured with 50 μL Protein A/G beads for 6 h at 4 °C (or overnight) and beads were collected (10,000 rpm, 5 min), washed four times with lysis buffer (NaCl, HEPES, sodium deoxycholate, Triton X-100, DTT, protease inhibitor cocktail 1:100, and Tris-HCl) at 4 °C (1 mL each; 14,000 rpm, 5 min) and twice with TE buffer; complexes were eluted with 100 μL elution buffer 1 at 65 °C for 10 min and then 150 μL elution buffer 2, pooling eluates (250 μL total), and crosslinks were reversed at 65 °C for 6 h or overnight; 10% eluate (25 μL) was reserved for optional Western blot, the remainder was treated with RNase A (20 μL; 100 mg/L) for 30 min at 37 °C and digested with proteinase K (250 μL of a proteinase K/glycogen mix prepared in TE) for 2 h at 58 °C, followed by DNA cleanup with 4 M LiCl (55 μL), phenol:chloroform:isoamyl alcohol extraction (25:24:1) and ethanol precipitation (−80 °C, 30 min; 14,000 rpm, 5 min, 4 °C), washing with 70% ethanol, air-drying, and resuspension in 25 μL nuclease-free water; DNA was quantified (Qubit) and stored at −20 °C. .. Immunoprecipitated DNA was subjected to other:Article Title: Nuclear GTPSCS functions as a lactyl-CoA synthetase to promote histone lactylation and gliomagenesis Article Snippet: Samples were then sent to Article Title: DMTF1 up-regulation rescues proliferation defect of telomere dysfunctional neural stem cells via the SWI/SNF-E2F axis Article Snippet: The library preparation and Purification:Article Title: Multi-omics dissection of the genetic regulation underlying fatty acid composition in cattle Article Snippet: DNA concentration was measured using Qubit® DNA Assay Kit in Qubit® 3.0 Fluorometer (Life Technologies, CA, USA). .. The purified DNA was used for Construct:Article Title: Multi-omics dissection of the genetic regulation underlying fatty acid composition in cattle Article Snippet: DNA concentration was measured using Qubit® DNA Assay Kit in Qubit® 3.0 Fluorometer (Life Technologies, CA, USA). .. The purified DNA was used for shRNA:Article Title: EPOP restricts PRC2.1 targeting to chromatin by directly modulating enzyme complex dimerization Article Snippet: .. For the |
