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Ab1791

Manufactured by Santa Cruz Biotechnology
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Sourced in United Kingdom
About the product

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.

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Lab products found in correlation

Ab2621, by Abcam (2 mentions) Clone c36b11, by Abcam (2 mentions) Ab8580, by Abcam (2 mentions) Ab8895, by Abcam (2 mentions) Sc 899, by Diagenode (2 mentions) Ab4441, by Diagenode (2 mentions) Ab10476, by Abcam (1 mentions) Sc 212, by Santa Cruz Biotechnology (1 mentions) Ab47774, by Abcam (1 mentions) Sc 59, by Santa Cruz Biotechnology (1 mentions) P50 sc 1191, by Santa Cruz Biotechnology (1 mentions) P65 ser486p, by Cell Signaling Technology (1 mentions) P65 ser536p, by Cell Signaling Technology (1 mentions) Iκb α ser32 36 9246, by Cell Signaling Technology (1 mentions) Hp4331, by ECM Biosciences (1 mentions) Hpa039441, by Abcam (1 mentions) Halt protease inhibitor, by Thermo Fisher Scientific (1 mentions) Sc 47724, by Santa Cruz Biotechnology (1 mentions) Sc 10252, by Proteintech (1 mentions) Ab6002, by Abcam (1 mentions)
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Similar products (other manufacturers)

Ab1791 (by Abcam) - 1611 citations Anti-Histone H3 (ab1791) (by Abcam) - 35 citations H3 (ab1791) (by Abcam) - 24 citations Ab1791 (by Fortrea) - 5 citations Ab1791 (by Proteintech) - 4 citations Ab1791-100 (by Abcam) - 4 citations Rabbit polyclonal anti-Histone H3 antibody (ab1791), (by Abcam) - 4 citations Rabbit anti-histone H3 (ab1791) (by Abcam) - 4 citations Ab1791 (by EASYBIO) - 3 citations Anti-H3 antibody (Ab1791; (by Abcam) - 3 citations

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21 protocols using «ab1791»

1

Western Blot Analysis of Nuclear Proteins

2023
Western blot analysis was performed on either total or nuclear protein fractions. Nuclear protein fractions were obtained by using Ne-PER Nuclear and Cytoplasmic Extraction Reagents following the manufacturer’s specification (Thermo Fisher Scientific 78833). Proteins were separated on NuPage 4-12% bis-tris gel (Thermo Fisher Scientific), and transferred to nitrocellulose membranes. The membranes were blotted with the following primary antibodies: anti-cleaved Caspase-7 (1 µg/ml, AbCam, ab2323), anti-ChK1 (phospho S317) (1:300, AbCam ab38518), anti-ChK1 (1:300, AbCam ab69536), anti-Nestin (1:300, Merck MAB353), anti-Neu (1:300, Merck MAB377), anti-H3 (1:10,000, AbCam ab1791), anti-Lamin B1 (Santa Cruz, sc-365214), anti-Claspin (1:300, Santa Cruz sc-376773 or sc-27297), and anti-DNA pol-β (1:300, Thermo Fisher Scientific MA5-13899). After washing in tris-buffered saline (TBS)/Tween 20X 0.1%, membranes were incubated with IRDye® 800CW goat anti-rabbit IgG or 680LT goat anti-mouse IgG secondary antibodies (1:15,000, LI-COR 926-32211 and 926-68020, respectively) for 1 hr at RT. Hybridization signals were detected with the Odyssey® Infrared Imaging System (LI-COR Biosciences) and quantified by freely available ImageJ software.
Caraci F., Fidilio A., Santangelo R., Caruso G., Giuffrida M.L., Tomasello M.F., Nicoletti F, & Copani A. (2023). Molecular Connections between DNA Replication and Cell Death in β-Amyloid-Treated Neurons. Current Neuropharmacology, 21(9), 2006-2018.
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2

Protein Expression Analysis by Western Blotting

2023
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.
Zhu K.G., Yang J., Zhu Y., Zhu Q., Pan W., Deng S., He Y., Zuo D., Wang P., Han Y, & Zhang H.Y. (2023). The microprotein encoded by exosomal lncAKR1C2 promotes gastric cancer lymph node metastasis by regulating fatty acid metabolism. Cell Death & Disease, 14(10), 708.
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3

Western Blot Analysis of Histone Modifications

2022
Proteins were separated by 4–20% SDS-PAGE (H3K27ac, H3K4me3, H3K4me1, H3, γ-tubulin) or 10% SDS-PAGE (LMNB1, γ-tubulin) and transferred to an Immobilon-FL membrane (Millipore). Membranes were blocked with Odyssey blocking buffer (LI-COR) (H3K27ac, H3K4me3, H3K4me1, H3) or 5 % milk (LMNB1, γ-tubulin) and incubated with antibodies against H3K4me1 (1:500; Abcam ab8895), H3K27ac (1:1000; Abcam 177178), H3K4me3 (1:1000; Diagenode Mab-152-050), H3 (1:1000; Abcam ab1791), LMNB1 (1:1000; Santa Cruz Biotechnology sc6216), or γ-tubulin (1:10000; Sigma-Aldrich T5326). Proteins were detected with IRDYE-800-coupled antibodies or Peroxidase-conjugated antibodies. Relative protein levels were quantified using Image Lab (BioRad) (https://www.bio-rad.com). Uncropped Western blots are shown in Additional file 1, Fig. S8.
Madsen-Østerbye J., Abdelhalim M., Baudement M.O, & Collas P. (2022). Local euchromatin enrichment in lamina-associated domains anticipates their repositioning in the adipogenic lineage. Genome Biology, 23, 91.
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4

Chromatin Immunoprecipitation and Sequencing

2022
Cells were crosslinked with either 2 mM ethylene glycol bis (succinimidyl succinate) (EGS, Pierce) for 45 min followed by a 1% formaldehyde for 20 min or 1% formaldehyde for 10 min before quenching with 250 mM glycine. Chromatin was released by sequential lysis with cells lysis buffer (10 mM Tris pH 8, 10 mM NaCl and 0.2% NP40) and nuclear lysis buffer (50 mM Tris pH 8, 10 mM EDTA and 1% SDS). Chromatin was sheared to ∼300 bp with 20 rounds of sonication (30 s on and 30 s off) on a Bioruptor (Diagenode) and a portion was kept as input. Chromatin was incubated overnight at 4 °C with 5 μg antibodies against either H3K9me3 (Abcam, ab8898), H3K36me3 (Abcam, ab9050), H3 (Abcam, ab1791), ATRX (Santa Cruz, SC15408), KDM4B (Abcam, ab191434) or H3.3 S31Ph (Active Motif) before immunoprecipitation with Protein A agarose beads (Sigma-Aldrich, 05015979001) and sequentially washing with low salt (20 mM Tris pH 8, 2 mM EDTA, 50 mM NaCl, 1% Triton X-100, 0.1% SDS), high salt (20 mM Tris pH 8, 2 mM EDTA, 500 mM NaCl, 1% Triton X-100, 0.01% SDS), LiCl buffers (10 mM Tris pH 8, 1 mM EDTA, 0.25 M LiCl, 1% NP40, 1% sodium deoxycholate) and TE buffer (10 mM Tris–HCl, 1 mM EDTA, pH 8). Chromatin was eluted with elution buffer (1% SDS, 100 mM NaHCO3), incubated with Proteinase K and de-crosslinked overnight at 65°C before phenol chloroform extraction and ethanol precipitation. Purified ChIP DNA was used as a template for qPCR with appropriate primers.
Udugama M., Vinod B., Chan F.L., Hii L., Garvie A., Collas P., Kalitsis P., Steer D., Das P.P., Tripathi P., Mann J.R., Voon H.P, & Wong L.H. (2022). Histone H3.3 phosphorylation promotes heterochromatin formation by inhibiting H3K9/K36 histone demethylase. Nucleic Acids Research, 50(8), 4500-4514.
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5

Enrichment and Analysis of Nuclear Proteins

2022
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 Data 1.
Xue S., Ly T.T., Vijayakar R.S., Chen J., Ng J., Mathuru A.S., Magdinier F, & Reversade B. (2022). HOX epimutations driven by maternal SMCHD1/LRIF1 haploinsufficiency trigger homeotic transformations in genetically wildtype offspring. Nature Communications, 13, 3583.
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Top 5 protocols citing «ab1791»

1

Chromatin Immunoprecipitation qPCR Analysis

Cited 2 times
Formaldehyde cross-linked chromatin was immunoprecipitated with IgG (Abcam, ab37415), anti-H3 (Abcam, ab1791), or anti-RNAPII (Santa Cruz Biotechnology, sc-9001) antibodies. Immunoprecipitated DNA was used as template for qPCR reactions after reversal of cross-links. See the Supplemental Material for details.
Hainer S.J., Gu W., Carone B.R., Landry B.D., Rando O.J., Mello C.C, & Fazzio T.G. (2015). Suppression of pervasive noncoding transcription in embryonic stem cells by esBAF. Genes & Development, 29(4), 362-378.
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2

Measuring JARID1B Protein Stability in PC3 Cells

Cited 1 time
Cell lysates were prepared in RIPA buffer (1×PBS, 1% Nonidet P40/Triton X-100, 0.5% sodium deoxycholate, 2mM EDTA, with or without 0.1% SDS) with protease inhibitor cocktail (Roche) followed with a brief sonication. Antibodies used were: rabbit anti-H3K4me3 (1:10,000, Cell Signaling, 9727), rabbit anti-H3 (1: 10,000, Abcam, Ab1791), rabbit anti-Skp2 (1:500, H-435, Santa Cruz, sc-7164), rabbit anti-JARID1B (1:10,000, Novus Biologicals, NB100-97821, NBP1-84352), mouse monoclonal anti-β-actin (1:10,000, Sigma, AC-74), mouse ant-Flag M2 affinity gel (Sigma, A2220), mouse anti-Flag M2 antibody (1:1000, Sigma, F1804), mouse anti-C-Myc (1:1000, Santa Cruz, sc-40), mouse anti-β-Galactosidase (1:1000, LSBio, 10B2), mouse anti-TRAF6 (1:1000, Santa Cruz, D-10), rabbit anti-TRAF6 (1:1000, Cell Signaling, D21G3). The protein stability of JARID1B in PC3 cells were performed as previously described [26 (link)]. PC3-scrambled and PC3-shSKP2 cells were incubated with 100 μg/ml of cycloheximide (CHX, Sigma) in starvation medium to inhibit further protein synthesis. To determine the stability of JARID1B proteins, cell lysates were collected at indicated time points after CHX treatment, and then subjected to Western blotting analysis using rabbit anti-JARID1B antibodies. Protein bands were quantified with Image J software. The protein degradation rate is represented as half-life (t1/2), which is defined as the time for 50% of the protein degraded.
Lu W., Liu S., Li B., Xie Y., Adhiambo C., Yang Q., Ballard B.R., Nakayama K.I., Matusik R.J, & Chen Z. (2014). SKP2 inactivation suppresses prostate tumorigenesis by mediating JARID1B ubiquitination. Oncotarget, 6(2), 771-788.
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3

Chromatin Immunoprecipitation (ChIP) Protocol

Cited 1 time
ChIP analysis was conducted according to the Hahn laboratory protocol (http://labs.fhcrc.org/hahn/Methods/mol_bio_meth/hahnlab_ChIP_method.html) with minor modifications. Briefly, DNA was fragmented by sonication to an average size of 400–500 bp for standard ChIP or 100–200 bp for high-resolution ChIP. Immunoprecipitation was conducted using Dynabeads Protein G (Invitrogen) and monoclonal antibodies against FLAG (Sigma-Aldrich; M2), Pk (AbD Serotec; SV5-Pk1) and Myc (Santa Cruz; 9E10); or polyclonal antibodies against histone H3 (Abcam; ab1791), Rap1 (Santa Cruz; yC-19) and Sua7 (in this study, raised against full-length recombinant Sua7 in rabbit). Real-time quantitative PCR analyses were performed using a KAPA SYBR Fast qPCR kit (KAPA) and Mx3000P (Agilent Technologies). PCR conditions were: 95°C for 40 s; 40 cycles of 95°C for 10 s, 52°C for 30 s and 72°C for 10 s. Each experiment was conducted in triplicate and the average and SD for the ratio of immunoprecipitated DNA versus input DNA (IP/input) was calculated. The positions of amplified regions are depicted in each figure. The primer pairs used for PCR are described in the Supplementary Data.
For sequential ChIP analysis, the first immunoprecipitation was performed as for standard ChIP analysis, except that 5 µg of anti-FLAG antibody and cell extracts containing 5 mg of protein were used. After a final wash with TE, precipitates were eluted by incubating beads with 50 µl of ChIP lysis buffer containing 3xFLAG peptide (200 µg/ml; Sigma-Aldrich; MDYKDHDGDYKDHDIDYKDDDDK) at 4°C for 30 min. Elution was performed four times in total, and the combined eluates were diluted with ChIP lysis buffer (to a concentration of 100 µg/ml 3xFLAG peptide), and were subjected to a second immunoprecipitation using an anti-Pk antibody. All steps after the second immunoprecipitation were the same as for standard ChIP analysis.
Kasahara K., Ohyama Y, & Kokubo T. (2011). Hmo1 directs pre-initiation complex assembly to an appropriate site on its target gene promoters by masking a nucleosome-free region. Nucleic Acids Research, 39(10), 4136-4150.
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4

Antibody Immunoblotting Protocol

Antibodies used were: anti-menin (Bethyl, A300-105A), anti-H3K4me3 (Abcam, ab-8580), anti-histone H3 (Abcam, ab-1791), anti-Gal4 (Santa Cruz, SC-510) and against HA (Roche, 3F10). Immunoblotting was carried out as described before (Dreijerink et al., 2006) .
Dreijerink K.M., Varier R.A., van Nuland R., Broekhuizen R., Valk G.D., van der Wal J.E., Lips C.J., Kummer J.A, & Timmers H.T. (2009). Regulation of vitamin D receptor function in MEN1-related parathyroid adenomas. Molecular and cellular endocrinology, 313(1-2).
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5

Proteomics Analysis of Stress Granule Proteins

Complete protease inhibitor cocktail was from Roche Inc. Dulbecco’s modified Eagle medium (DMEM) minus l-arginine and l-lysine, dialyzed fetal calf serum (dFCS) and trypsin were from Thermo Scientific. Stably isotope labeled l-arginine and l-lysine were from Cambridge Isotope Laboratories. All other chemicals were from Sigma Aldrich. Full-length ASCC3 with a C-terminal HA-tag and CFP-DCP1A have been described previously [44 (link), 45 (link)].
Primary antibodies and dilutions: ALKBH3 (Santa Cruz, sc-376520, IF: 1/100, WB: 1/2000), ASCC3 (Atlas, HPA001439, IF: 1/50), β-actin (Abcam, ab8226, IB: 1/2000), CELF1 (Santa Cruz, SC-20003, IB: 1/1000, IF: 1/200), EIF2S1 (Atlas, HPA064885, IB: 1/1000), EIF2S1-pS51 [Abcam, ab32157, IB: 1/500. Note that in the canonical human EIF2S1 sequence, this serine is at position 52 (UniProtKB-P05192)], HA-tag (Santa Cruz, SC-805, IF: 1/100). Histone H3 (Abcam, ab1791, IB: 1/2000), HNRNPA1 (Santa Cruz Biotechnology, SC-32301, IB: 1/3000, IF: 1/200), RPS10 (Atlas, HPA048084, IB: 1:125), RPL18 (Atlas, HPA046572, IB: 1:250), SERBP1 (Sigma, WH0026135M1, IB: 1/1000, IF: 1/50), SND1 (Sigma, HPA002632, IB: 1/1000, IF: 1/50), TIA1 (Abcam, ab196382, IF: 1/100), HRP-conjugated swine anti-rabbit (P0399) and rabbit anti-mouse (P0260) secondary antibodies were from Dako Chemicals. IRDye® 680RD Goat anti-Mouse IgG and IRDye® 680RD Goat anti-Rabbit IgG secondary antibodies were from LiCor Biotechnology. Secondary antibodies for confocal microscopy were from Life Technologies; Alexa Fluor® 488 rabbit anti-mouse (#A-11059) and donkey anti-rabbit (#A-21206), Alexa Fluor® 532 goat anti-mouse (#A-11002) and goat anti-rabbit (#A-11009), Alexa Fluor® 647 donkey anti-goat (#A-21477) and goat anti-rabbit (#A-21244).
Wollen K.L., Hagen L., Vågbø C.B., Rabe R., Iveland T.S., Aas P.A., Sharma A., Sporsheim B., Erlandsen H.O., Palibrk V., Bjørås M., Fonseca D.M., Mosammaparast N, & Slupphaug G. (2021). ALKBH3 partner ASCC3 mediates P-body formation and selective clearance of MMS-induced 1-methyladenosine and 3-methylcytosine from mRNA. Journal of Translational Medicine, 19, 287.
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