Immunoblotting of whole Jurkat T cell lysates or nuclear extracts (Sutcliffe et al., 2012 (link)) was performed with: anti-PKC-θ (sc-212, Santa Cruz Biotechnology), anti-PKC-θ S676p (ab47774, Abcam), p65 (ab7970, Abcam), H3 (ab1791), Sp-1 (sc-59, Santa Cruz Biotechnology), p50 (sc-1191, Santa Cruz Biotechnology), p65 Ser486p (3039, Cell Signaling Technology), p65 Ser536p (3031, Cell Signaling Technology), IκB-α (Ser32/36; 9246, Cell Signaling Technology), H2B Ser32p (ab10476, Abcam), and H2B Ser36p (ECM Biosciences HP4331) antibodies with a dilution range of 1:200 to 1:1000. Signals were detected by enhanced chemiluminescence on a LAS4000 Fluoimager.
Ab1791
Manufactured by Santa Cruz Biotechnology
Sourced in United Kingdom
Ab1791 is a laboratory equipment product manufactured by Santa Cruz Biotechnology. It is designed for use in various research and scientific applications. The core function of Ab1791 is to facilitate the analysis and detection of specific biomolecules or cellular components. Further details about its intended use or specific applications are not available.
Automatically generated - may contain errors
Lab products found in correlation
Steponeplus real time pcr system, by Thermo Fisher Scientific (2 mentions)
Ab4441, by Diagenode (2 mentions)
Absolute qpcr rox mix, by Thermo Fisher Scientific (2 mentions)
Sc 899, by Diagenode (2 mentions)
Immobilon, by Merck Group (2 mentions)
Ab8895, by Abcam (2 mentions)
Clone c36b11, by Abcam (2 mentions)
Ab2621, by Abcam (2 mentions)
Ab10476, by Abcam (1 mentions)
Sc 59, by Santa Cruz Biotechnology (1 mentions)
Ab4729, by Abcam (1 mentions)
Ab8580, by Abcam (1 mentions)
Ab6002, by Abcam (1 mentions)
Image station 4000r, by Kodak (1 mentions)
Ab3181, by Abcam (1 mentions)
Ab10362, by Abcam (1 mentions)
Sc 56, by Santa Cruz Biotechnology (1 mentions)
Ta503755, by OriGene (1 mentions)
Halt protease inhibitor, by Thermo Fisher Scientific (1 mentions)
Hpa039441, by Abcam (1 mentions)
16 protocols using ab1791
1
Immunoblotting of Jurkat T Cell Lysates
2
ChIP-qPCR Analysis of Histone Modifications
3
HSV-1 Infection Alters Histone Modifications
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HeLa cells infected by HSV-1 were lysed in ice-cold whole-cell extract buffer B (50 mM TRIS-HCl, pH 8.0, 4 M urea, and 1% Triton X-100), supplemented with complete protease inhibitor mixture. Cell extracts resolved by SDS-PAGE were analyzed by western blotting. Protein bands were visualized using ECL Blotting Detection Reagents. Antibodies used for western blotting include anti-H3K4Me3 antibodies (Abcam, ab8580), anti-H3K27Me3 antibodies (Abcam, ab6002), anti-H3K27Ac antibodies (Abcam, ab4729), anti-histone H3 antibodies (Abcam, ab1791), anti-SRSF2 (Santa Cruz Biotechnology, sc-10252), and anti-beta-actin antibodies (Proteintech, 60008-1-Ig).
4
Western Blot Analysis of DNA Repair Proteins
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Proteins were transferred to PVDF-membranes (Immobilon, Millipore) and the membranes were blocked in 5% dry milk in PBS-T before incubation with primary antibodies in 5% dry milk. Antibodies against POLβ (ab3181), POLδ (ab10362, Abcam), XRCC1 (ab1838), LIG1 (ab615), LIG3 (ab587), H3 (ab1791), PCNA (SC-56, Santa-Cruz Biotechnology), FEN1 (A300-256, Bethyl Laboratories) and α-UNG2 (TA503755, OriGene) were used. Membranes were incubated in swine α-rabbit and rabbit α-mouse secondary antibodies (Dako Cytomation) diluted 1:5000 in 1% dry milk and visualized in KODAK Image Station 4000R.
5
Enrichment and Analysis of Nuclear Proteins
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Zebrafish embryos at sphere stage were dechorionated using 1 mg/ml pronase and deyolked as previously described37 (link). To enrich for nuclear proteins, embryos were lysed in hypotonic lysis buffer (10 mM Tris pH7.5, 10 mM NaCl, 3 mM MgCl2, 0.3% NP40, 10% glycerol, 1x Protease inhibitor) for 10 min on ice and centrifuged 800 g for 8 min. The supernatant containing cytoplasmic fraction was discarded. The pellet containing nuclear proteins was resuspended in MWB (10 mM Tris pH: 7.5, 300 mM NaCl, 4 mM EDTA, 1% NP40, 10% glycerol, TURBO DNase, 1x Protease Inhibitor). Nuclear proteins from 300 embryos were loaded per lane. Human fibroblasts and mouse embryo heads were lysed in RIPA buffer (250 mM Tris, pH: 7.5; 150 mM NaCl; 1% NP-40; 0.5% Na deoxycholate, Halt protease inhibitors [Thermo]). Immunoblotting was performed using the following antibodies: anti-SMCHD1 (Atlas HPA039441, 1:500), anti-Histone H3 (abcam ab1791, 1:1000), anti-GAPDH (Santa Cruz SC47724, 1:1000).
In situ hybridization Probes for in situ hybridisation were cloned from zebrafish embryo cDNA using primers in Supplementary Data1 .
In situ hybridization Probes for in situ hybridisation were cloned from zebrafish embryo cDNA using primers in Supplementary Data
6
Protein Expression Analysis by Western Blotting
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The protein levels of CPT1A, Flag-pep-AKR1C2, pep-AKR1C2, YAP, p127-YAP, VEGFC and HIF-1α were assessed by western blotting analysis and samples were normalized to GAPDH. For animals, mice were firstly sacrificed with carbon dioxide asphyxiation. Protein extraction was blocked with PBS-5% fat-free dried milk at room temperature for 1 h and incubated at 4 °C overnight with anti-CPT1A (1:1000; Abcam, Cambridge, UK; ab234111), anti-Flag (1:5,000; Abcam, Cambridge, UK; ab205606), anti-YAP (1:1000, Abcam; ab205270), anti p127-YAP (1:1000, Abcam; ab76252), anti-pep-AKR1C2 (1:1000, CST, 13035 S), anti-VEGFC (1:1000, Abcam; ab9546), anti-HIF-1α (Santa Cruz, sc-13515) anti-TSG101 (1:200; Santa Cruz, sc-7964), anti-Alix (1:1000, Abcam, ab275377), anti-CD9 (1:1000, Abcam, ab223052), anti-H3 (1:1000, Abcam, ab1791) and anti-GAPDH (1:3000, Santa Cruz, sc-365062) antibodies respectively.
7
Western Blot Analysis of Autophagy and Cell Signaling
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Tissue samples were homogenised with the Precellys 24 tissue homogeniser in Laemmli buffer and samples ran on 12.5 or 15% gels. Protein was transferred to PVDF membranes (Immobilon, Millipore), which was subsequently blocked for 1 h at room temperature (5% milk solution in TBS-Tween 0.1%) before incubating with primary antibody at 4 °C overnight. An appropriate HRP-conjugated secondary antibody was incubated at room temperature for 1 h. Western blots were visualised with chemiluminescence reagents (Sigma, RPN2106). Antibodies were used at the following concentrations: Anti-ATG5 (Abcam, ab108327; 1:1000), anti-LC3 (Abcam, ab192890; 1:1000), anti-ACTIN (Santa Cruz Biotechnology, I-19; 1:5000 [no longer commercially available]), anti-P53 (Cell Signalling Technologies, Clone 1C12; 1:1000), anti-P21 (Santa Cruz, SC-6246; 1:1000), anti-Histone H3 (Abcam, ab1791; 1:5000), anti-P16 (Santa Cruz, SC-1207; 1:1000), anti-HMGA1 (Abcam, ab129153; 1:1000), anti-NBR1 (Abcam, ab55474; 1:1000).
8
Histone Modification Analysis by Western Blot
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Whole-cell lysate was prepared in 3D-RIPA buffer. Protein (20 µg) was separated by 12% SDS–PAGE and transferred to a polyvinylidene difluoride membrane. Membranes were blocked using 5% nonfat dry milk in PBS containing 0.05% Tween 20, and then incubated with primary antibody overnight at 4 °C. HRP-conjugated secondary antibody was used and detected using the Pierce ECL Western Blot Substrate. Antibodies were obtained from the following sources: H3K9Ac (Abcam, ab32129, 1:1000), H3K4Me2 (Abcam, ab32356, 1:5000), H3K4Me1 (Abcam, ab8895, 1:5000), H3K4Me3 (Abcam, ab8580, 1:5000), H3K14Ac (Millipore, 07–353, 1:5000), H3K18Ac (Millipore, 07–354, 1:5000), LSD1 (Abcam, ab17721, 1:500), HDAC1 (Abcam, ab19845, 1:1000), total H3 (Cell Signaling Technology, 4499 S, 1:1000 or Abcam, ab1791, 1:10,000), β-actin (Santa Cruz Biotechnology, sc47778, 1:2000), CoREST1 (BD Transduction Laboratories, 612146, 1:500), SIN3A (Abcam, ab129087, 1:1000), HRP-conjugated secondary antibodies (Santa Cruz Biotechnology, 1:5000 for β-actin blots, 1:2000 for all others). Blots shown are representative of at least two independent experiments. Uncropped versions of Western blots are provided in the Supporting Information (Supplementary Figs. 32 and 33 ).
9
ChIP-qPCR Analysis of Histone Modifications
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ChIP experiments were performed as previously described (Oswald et al., 2016 (link)). The following antibodies were used: anti-H3K9ac (abcam, ab4441), anti-H3K27ac (Diagenode, pAb-174–050), anti-H3 (abcam, ab1791), anti-RNAPII (Santa Cruz, sc-899) or IgG (Diagenode, C15410206) as mock control. Experiments were analyzed by qPCR on a StepOnePlus Real-Time PCR System (Applied Biosystem), making use of Absolute QPCR ROX Mix (Thermo Scientific AB-1139), gene-specific oligonucleotides and double-dye probes (see Key Resources Table ). Gene desert was used as negative control as previously described (Oswald et al., 2016 (link)).
10
Histone Methylation Analysis in Leukemia
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1×106 NUP98-NSD1 and HM-2 cells in required medium with 10% FBS and 1% Pen Strep were collected, washed, and whole cell lysate was prepared using RIPA lysis buffer supplemented with 1X proteinase inhibitor cocktail. For compound-treated samples, 1×105 NUP98-NSD1 cells or 1×104 HM-2 cells in required medium with 10% FBS and 1% Pen Strep were seeded in 24-well culture plates in 1 ml medium and treated with indicated doses of BT5 for 4 days. Cells were collected, counted and re-plated at initial cell density with fresh medium and compound for another 4 days. On day 8, cells were collected, washed, and whole cell lysate was prepared using RIPA lysis buffer supplemented with 1X proteinase inhibitor cocktail. Western blot detection of histone H3K36me2 (Cell signaling technology #2901S, clone CZ5H12, dilution 1:2,000), histone H3K36me3 (Cell signaling technology, #4909S, clone D5A7, dilution 1:2,000), histone H3K27me3 (Cell signaling technology, #9733S, clone C36B11, dilution 1:2,000), H3K79me3 (abcam, #ab2621, dilution 1:2,000) was performed using 12% SDS-PAGE gel. Total H3 (abcam, #ab1791, dilution 1:50,000) and Actin (Santa Cruz, #sc-47778, dilution 1:10,000 or Genescript, #A00702, dilution 1:10,000) were used as loading controls.
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