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Histone H1

Histone H1 is a member of the histone protein family, which play a crucial role in the structural organization of chromatin within the eukaryotic cell nucleus.
As a linker histone, Histone H1 helps condense DNA into higher-order chromatin structures, regulating gene expression and chromosomal stability.
Understanding the functions and interactions of Histone H1 is essential for advancing research in areas such as epigenetics, cell biology, and developmental biology.
PubCompare.ai's AI-driven platform can streamline your Histone H1 research by helping you locate the best protocols from literature, pre-prints, and patents, using advanced comparisons to ensure reproducibble and accurate findings.

Most cited protocols related to «Histone H1»

1
Quantifying SOMAmer-Protein Dissociation Kinetics
Cited 18 times
The rate constant for SOMAmer:protein complex dissociation was determined for each aptamer by measuring the fraction of pre-formed aptamer:protein complexes that remain bound after addition of a competitor as a function of time. Radiolabled SOMAmer was renatured as described above. Approximately 5×10–11 M SOMAmer was equilibrated in SB18T (40 mM HEPES, 100 mM NaCl, 5 mM KCl, 5 mM MgCl2, 0.05% Tween-20 at pH 7.5) at 37°C with protein at a concentration 10X greater than the measured Kd value. Samples were then diluted 2X with 40 nM non-labeled SOMAmer or 0.3 mM dextran sulfate in SB18T at various time points. Complexes were partitioned to separate free aptamer from protein:aptamer complexes. The type of partitioning was dependent upon the protein used since not all proteins bind to the same type of partitioning resin. For LBP and Histone H1.2, Zorbax PSM-300A (Agilent Technologies) resin was used for partitioning; for Kallistatin, MyOne TALON beads were used; for biotinylated-TIG2, MyOne Streptavidin beads were used. Complexes were captured on the appropriate resin, and the sample was passed through a MultiScreen HV Plate under vacuum. The samples were washed with SB18T. The MultiScreen HV Plates were phosphorimaged and the amount of radioactivity in each sample quantified using a FUJI FLA-3000. The fraction of complex remaining was plotted as a function of time, and the dissociation rate constant was determined by fitting the data to an analytic expression for bimolecular dissociation kinetics using non-linear regression.
Gold L., Ayers D., Bertino J., Bock C., Bock A., Brody E.N., Carter J., Dalby A.B., Eaton B.E., Fitzwater T., Flather D., Forbes A., Foreman T., Fowler C., Gawande B., Goss M., Gunn M., Gupta S., Halladay D., Heil J., Heilig J., Hicke B., Husar G., Janjic N., Jarvis T., Jennings S., Katilius E., Keeney T.R., Kim N., Koch T.H., Kraemer S., Kroiss L., Le N., Levine D., Lindsey W., Lollo B., Mayfield W., Mehan M., Mehler R., Nelson S.K., Nelson M., Nieuwlandt D., Nikrad M., Ochsner U., Ostroff R.M., Otis M., Parker T., Pietrasiewicz S., Resnicow D.I., Rohloff J., Sanders G., Sattin S., Schneider D., Singer B., Stanton M., Sterkel A., Stewart A., Stratford S., Vaught J.D., Vrkljan M., Walker J.J., Watrobka M., Waugh S., Weiss A., Wilcox S.K., Wolfson A., Wolk S.K., Zhang C, & Zichi D. (2010). Aptamer-Based Multiplexed Proteomic Technology for Biomarker Discovery. PLoS ONE, 5(12), e15004.
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Publication 2010
Claw HEPES Histone H1 kallistatin Kinetics Magnesium Chloride Protein C Proteins Radioactivity Resins, Plant Sodium Chloride Streptavidin Sulfate, Dextran Tween 20 Vacuum
2
Characterizing NF-κB Transcriptional Regulation
Cited 13 times

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Publication 2011
2',5'-oligoadenylate anti-IgG Biological Assay Cells Checkpoint Kinase 1 DNA Chips Electrophoretic Mobility Shift Assay Genotoxic Stress HEK293 Cells Histone H1 Homo sapiens Immunoblotting Luciferases oligofectamine Oligonucleotide Primers Oligonucleotides Phosphotransferases RNA Polymerase II Sea Pansy Transfection
3
Synthesis and Purification of PAR
Cited 13 times
According to Kiehlbauch et al. (19 (link)), PAR was synthesized with some modifications. Briefly, PAR was synthesized in a 20 ml incubation mixture comprising 100 mM Tris–HCl pH 7.8, 10 mM MgCl2, 1 mM NAD+, 10 mM DTT, 60 μg/ml histone H1, 60 μg/ml histone type IIa, 50 μg/ml octameric ‘activator’ oligonucleotide GGAATTCC and 150 nM human PARP-1. The reaction was stopped after 15 min by addition of 20 ml ice-cold 20% TCA. Following precipitation the pellet was washed with ice-cold 99.8% ethanol. Polymer was detached using 0.5 M KOH/50 mM EDTA and purified as described (36 (link)). After extraction with phenol–chloroform–isoamyl alcohol PAR was precipitated with ethanol overnight. Following centrifugation PAR was air-dried and stored at −20°C
Fahrer J., Kranaster R., Altmeyer M., Marx A, & Bürkle A. (2007). Quantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain length. Nucleic Acids Research, 35(21), e143.
Publication 2007
Centrifugation Chloroform Cold Temperature Edetic Acid Ethanol Histone H1 Histones Homo sapiens isopentyl alcohol Magnesium Chloride Oligonucleotides PARP1 protein, human Phenol Polymers Tromethamine
4
PPARγ Phosphorylation Assay
Cited 11 times
Immuno-purified WT or S273A mutant of PPARγ were incubated with active cdk kinases in kinase assay buffer containing ATP for 15 min at 30°C. Positive controls, either purified histone H1 (Millipore) or Rb (Cell Signaling Technology) were used. Several PPARγ ligands were pre-incubated with substrates for 30 min before the assay was performed.
Choi J.H., Banks A.S., Estall J.L., Kajimura S., Bostrom P., Laznik D., Ruas J.L., Chalmers M.J., Kamenecka T.M., Bluher M., Griffin P.R, & Spiegelman B.M. (2010). Obesity-linked phosphorylation of PPARγ by cdk5 is a direct target of the anti-diabetic PPARγ ligands. Nature, 466(7305), 451-456.
Publication 2010
Biological Assay Buffers Histone H1 Ligands Phosphotransferases Phosphotransferases, ATP PPAR gamma
5
Reconstituting Nucleosome Templates for RNAP Stalling
Cited 11 times
We gel-purified the 149-bp and 249-bp DNA fragments, used them for nucleosome reconstitution by octamer exchange at 1:3 DNA:chromatin ratio17 (link). The hexasomes were reconstituted using chicken erythrocytes core histones by dialysis from 2 M NaCl48 (link).
To obtain 603-42 and 603-49 templates for E. coli RNAP we mutated the original 603 template to replace four or six nucleotides in DNA and allow stalling of RNAP at the +42 or +49 positions within the 603 nucleosome, respectively. We amplified the nucleosome positioning sequences by PCR, digested by TspRI (NEB) and ligated through the TspRI site to a T7A1 promoter-bearing fragment30 (link). Ligated products were re-amplified with one 5′-end-labeled primer, gel-purified, and assembled into nucleosomes. We reconstituted nucleosomes on the DNA templates by histone octamer transfer from chicken -H1 erythrocyte donor chromatin17 (link).
Kulaeva O.I., Gaykalova D.A., Pestov N.A., Golovastov V.V., Vassylyev D.G., Artsimovitch I, & Studitsky V.M. (2009). Mechanism of chromatin remodeling and recovery during passage of RNA polymerase II. Nature structural & molecular biology, 16(12), 1272-1278.
Publication 2009
Chickens Chromatin Dialysis Erythrocytes Escherichia coli Histone H1 Histones Nucleosomes Nucleotides Oligonucleotide Primers Tissue Donors

Most recents protocols related to «Histone H1»

1
Synthesis and Characterization of Poly(ADP-ribose)
Synthesis of PAR was performed as previously reported20 (link). Briefly, 50 units of purified human PARP-1 (High Specific Activity hPARP-1, Trevigen) were incubated in a mixture containing 100 mM Tris-HCl pH 8, 10 mM MgCl2, 2 mM dithiothreitol, 2.5 μg of DNase I-activated calf thymus DNA (Trevigen) and 200 mM NAD+ (Sigma-Aldrich) for 45 min at 30 °C. The reaction was stopped by adding ice-cold trichloroacetic acid (TCA) to a final concentration of 20% (w/v). PARs were detached from proteins by incubation in 50 mM NaOH and 10 mM EDTA for 1 hr at 60 °C. After adjustment of pH to 7.5, PAR were purified by phenol/chloroform extraction as described20 (link).
For the study of non-covalent interaction of PAR with TRF-1, graded concentrations of purified His-hTRF1 protein were immobilized directly by slot-blotting on nitrocellulose membranes. Histone H1 (Millipore) was used as positive control in the PAR binding assay. Subsequently, filters were incubated with PAR diluted in TBS-T (10 mM Tris-HCl pH 8.0, 150 mM NaCl, 0.1% Tween 20) for 1 hr at room temperature. After high-stringency salt washes, protein bound PAR were detected using the anti-PAR monoclonal antibody (mouse Mab ALX-804220).
Maresca C., Dello Stritto A., D’Angelo C., Petti E., Rizzo A., Vertecchi E., Berardinelli F., Bonanni L., Sgura A., Antoccia A., Graziani G., Biroccio A, & Salvati E. (2023). PARP1 allows proper telomere replication through TRF1 poly (ADP-ribosyl)ation and helicase recruitment. Communications Biology, 6, 234.
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Publication 2023
Anabolism Antibodies, Anti-Idiotypic Biological Assay calf thymus DNA Chloroform Cold Temperature Deoxyribonuclease I Dithiothreitol Edetic Acid Histone H1 Homo sapiens Magnesium Chloride Mice, House Nitrocellulose PARP1 protein, human Phenol Poly(ADP-ribose) Polymerases Proteins Sodium Chloride Tissue, Membrane Trichloroacetic Acid Tromethamine Tween 20
2
Polyclonal Antibody Production for Cnidarian Nematocyst Proteins
For the gastrozooid-expressed JFT, HsymJFT1c-I, polyclonal antibodies were produced by AbClonal using their Rabbit Polyclonal Antibody Development For Protein service. For the dactylozooid-specific JFT, HsymJFT1c-II, polyclonal antibody was designed, expressed, and purified from GenScript Biotech using their PolyExpress Premium Antigen-Specific Affinity Purified pAb service. Goat anti-rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody Alexa Fluor 594 (Invitrogen, Cat. A-11012) was used as the secondary antibody. Anti-human Histone H1 (Leinco Technologies Inc. Prod. # H126) and Goat anti-mouse IgG (H+L), F(ab%)2 fragment, CF 488A antibody Secondary Alexa (Sigma-Aldrich, Cat. SAB4600388) were used as controls. Immunostaining was carried out as in Sanders et al. [41 (link)]. The DAPI staining occurred in 9:1 glycerol/PBS media, which reduces the staining in capsules of maturing and mature nematocysts. Epifluorescence images were taken using a Leica DM5000 B with attached Lumenera Infinity 3s and Infinity Analyze v7 software. Confocal images were taken either using a Leica Laser Scanning Confocal Upright Microscope at the University of Kansas Microscopy and Analytical Imaging Core or LeicaTCS SP5 with LAS AF software. Images were processed using Fiji (ImageJ2) v2.9.0/1.53t [46 (link)] and all final figures were designed using Inkscape [40 ]. An alignment of all studied JFTs in this work shows antigentic regions selected for antibody production in Supplementary Figure S5 [47 (link),48 (link)]. A lack of HsymJFT1c-II staining in gastrozooids is shown in Supplementary Figure S6.
Klompen A.M., Travert M.K, & Cartwright P. (2023). Localization of Multiple Jellyfish Toxins Shows Specificity for Functionally Distinct Polyps and Nematocyst Types in a Colonial Hydrozoan. Toxins, 15(2), 149.
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Publication 2023
Alexa594 anti-IgG Antibodies Antibody Formation Antigens Capsule Cytochrome P-450 CYP2B1 DAPI Glycerin Goat Histone H1 Homo sapiens Immunoglobulins Microscopy, Confocal Mus Nematocyst Proteins Rabbits
3
Fluorescently Tagged HeLa Cell Line
Cited 1 time
HeLa cells with endogenous tagging with fluorescent proteins of β-tubulin (mClover3), histone H1 (mTagBFP2), and p62-SQSTM1 (mRuby3) were developed with CRISPR and the FAST-HDR vector system, and were recently described [17 (link)]. These cells are commercially available from ExpressCells, Inc. A clonal cell line was derived by single cell sorting with the Hana Single Cell Sorter Instrument (Namocell) using the green fluorescent channel and sorting into a 96 well plate. Single cell clones were analyzed with a Spark Cyto plate reader (Tecan) using whole-well imaging for selecting clones derived from a single cell. A clone with uniform and bright β-tubulin fluorescence was selected to expand a cell line for this study.
Khachatryan H., Olszowy B., Barrero C.A., Gordon J, & Perez-Leal O. (2023). Identification of Inhibitors of Tubulin Polymerization Using a CRISPR-Edited Cell Line with Endogenous Fluorescent Tagging of β-Tubulin and Histone H1. Biomolecules, 13(2), 249.
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Publication 2023
Cell Lines Cells Clone Cells Cloning Vectors Clustered Regularly Interspaced Short Palindromic Repeats Fluorescence HeLa Cells Histone H1 Proteins Tubulin
4
Haralick Texture Analysis of Cytoplasm
For image data analysis, we used Harmony Software 4.8 (Perkin Elmer). The analysis was conducted using the following steps within the Analysis module of Harmony Software: (1) identifying the cell nucleus with the “Find Nuclei” algorithm using the Histone H1-mtagBFP2 channel, (2) detecting the cytoplasm boundaries of the identified cell nucleus using the “Find Cytoplasm” algorithm with the TUBB-mClover3 channel, and (3) analyzing the texture properties of the cytoplasm of each cell using the Haralick analysis option with default settings. The Haralick texture analysis option provides values for pixel correlation, contrast, homogeneity, and sum variance. For this study, we only evaluated changes in the mean pixel homogeneity values per each well.
Khachatryan H., Olszowy B., Barrero C.A., Gordon J, & Perez-Leal O. (2023). Identification of Inhibitors of Tubulin Polymerization Using a CRISPR-Edited Cell Line with Endogenous Fluorescent Tagging of β-Tubulin and Histone H1. Biomolecules, 13(2), 249.
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Publication 2023
Cell Nucleus Cytoplasm Histone H1
5
Protein Extraction and Western Blot Analysis
Total protein and nuclear protein were extracted from cells and murine tissues. The protein concentration was detected by using a BCA protein assay kit. Equal amounts of protein (25 μg) were separated on SDS-PAGE gel and electro-transferred onto a polyvinylidene difluoride membrane (PVDF). Next, PVDF membranes were blocked with 5% fat-free milk for 1 h, and then incubated with primary antibodies overnight at 4 °C. After incubating with secondary antibodies at room temperature, the optical density of the bands was visualized by an ECL system (Pierce). Data was normalized to GAPDH or Histone H1 levels.
Xue X., Li F., Xu M., Chen B., Zhao Y., Wang M, & Li L. (2023). Gastrodin ameliorates atherosclerosis by inhibiting foam cells formation and inflammation through down-regulating NF-κB pathway. Nutrition & Metabolism, 20, 9.
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Publication 2023
Antibodies Biological Assay Cardiac Arrest GAPDH protein, human Histone H1 Milk, Cow's Mus Nuclear Protein polyvinylidene fluoride Proteins SDS-PAGE Tissue, Membrane Tissues Vision

Top products related to «Histone H1»

1
Histone h1 by Santa Cruz Biotechnology
Sourced in United States, Canada
Histone H1 is a protein found in the nucleus of eukaryotic cells. It is responsible for the compaction of DNA into higher-order chromatin structures, playing a crucial role in the regulation of gene expression and DNA organization within the cell.
2
Histone h1 by Merck Group
Sourced in Macao, United States, Germany
Histone H1 is a type of histone protein found in the nuclei of eukaryotic cells. It plays a role in the structural organization of chromatin by facilitating the formation of higher-order chromatin structures.
3
β actin by Santa Cruz Biotechnology
Sourced in United States, United Kingdom, China, Germany, Canada, Morocco, Japan, Italy, Switzerland, France, Israel, Singapore, Hong Kong, Sweden, Macao, Panama
β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is a component of the microfilament system and plays a crucial role in various cellular processes, such as cell motility, maintenance of cell shape, and intracellular trafficking.
4
Histone h1 by Roche
Sourced in Germany
Histone H1 is a type of histone protein found in eukaryotic cells. Histones are essential components of chromatin, the complex of DNA and proteins that make up chromosomes. Histone H1 plays a role in the organization and compaction of chromatin structure.
5
Gapdh by Santa Cruz Biotechnology
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GAPDH is a housekeeping gene that encodes the enzyme glyceraldehyde 3-phosphate dehydrogenase, which is involved in the glycolytic pathway. This enzyme catalyzes the oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate.
6
γ 32p atp by PerkinElmer
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[γ-32P]ATP is a radiolabeled compound containing the radioactive isotope phosphorus-32 (32P) attached to the gamma phosphate group of adenosine triphosphate (ATP). This product is commonly used as a tracer in various biochemical and molecular biology applications, such as nucleic acid labeling and analysis.
7
Anti histone h1 by Santa Cruz Biotechnology
Sourced in United States
Anti-histone H1 is a laboratory reagent used for the detection and analysis of histone H1 proteins. Histone H1 is a type of linker histone that plays a role in the organization and compaction of chromatin within the cell nucleus. This antibody can be used in various experimental techniques, such as Western blotting, immunohistochemistry, and immunoprecipitation, to study the expression and localization of histone H1 proteins.
8
β actin by Merck Group
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β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.
9
Anti histone h1 by Abcam
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Anti-Histone H1 is a laboratory reagent used for the detection and analysis of histone H1 proteins. Histone H1 is a class of histone proteins responsible for the compaction of chromatin in eukaryotic cells. This product can be used in various techniques, such as Western blotting and immunohistochemistry, to study the expression and distribution of histone H1 proteins.
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Bcl-2 is a lab equipment product that serves as a key regulator of apoptosis, or programmed cell death. It plays a crucial role in controlling the balance between cell survival and cell death. The core function of Bcl-2 is to inhibit apoptosis, thereby promoting cell survival.

More about "Histone H1"

Histone H1 is a member of the histone protein family, which play a crucial role in the structural organization of chromatin within the eukaryotic cell nucleus.
As a linker histone, Histone H1 helps condense DNA into higher-order chromatin structures, regulating gene expression and chromosomal stability.
Understanding the functions and interactions of Histone H1 is essential for advancing research in areas such as epigenetics, cell biology, and developmental biology.
Histone H1, also known as H1 histone or H1 histoone, is a type of histone protein that binds to the linker DNA between nucleosomes, helping to condense and stabilize the chromatin structure.
It is one of the five main histone proteins (H1, H2A, H2B, H3, and H4) found in eukaryotic cells.
The Histone H1 protein is involved in a variety of cellular processes, including transcriptional regulation, chromatin remodeling, and chromosome organization.
It plays a key role in the compaction of DNA into higher-order chromatin structures, which can impact gene expression and genomic stability.
Researchers studying Histone H1 often use techniques such as Western blotting, immunoprecipitation, and chromatin immunoprecipitation (ChIP) to investigate its localization, interactions, and functions.
Common antibodies used in Histone H1 research include Anti-histone H1 and Anti-Histone H1.
In addition to Histone H1, other proteins like β-actin and GAPDH are often used as reference or housekeeping genes in molecular biology experiments.
The radioactive compound [γ-32P]ATP can also be utilized to study the phosphorylation and dynamic behavior of Histone H1 and other chromatin-associated proteins.
By leveraging PubCompare.ai's AI-driven platform, researchers can streamline their Histone H1 studies by accessing the best protocols from literature, pre-prints, and patents, ensuring reproducible and accurate findings.
This can help advance our understanding of the crucial role Histone H1 plays in epigenetics, cell biology, and developmental processes.