05-928
Anti-Histone H3 Antibody, CT, pan, clone A3S, rabbit monoclonal
clone A3S, Upstate®, from rabbit
Synonym(s):
H3, Histone H3, H3 histone, family 3A
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
A3S, monoclonal
species reactivity
Saccharomyces cerevisiae, mouse, chicken, yeast, human, rat
manufacturer/tradename
Upstate®
technique(s)
ChIP: suitable
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... H3F3B(3021)
General description
Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ′beads on a string′ structure.
Specificity
Broad species cross-reactivity expected due to sequence homology.
Recognizes Histone H3, Mr 17 kDa
Immunogen
KLH-conjugated, synthetic peptide corresponding to the C-terminus of human Histone H3.
Application
Chromatin Immunoprecipitation:
2 μL of this antibody immunoprecipitated chromatin associated with Histone H3 from a wild type yeast lysate.
2 μL of this antibody immunoprecipitated chromatin associated with Histone H3 from a wild type yeast lysate.
Use Anti-Histone H3 Antibody, CT, pan, clone A3S (Rabbit Monoclonal Antibody) validated in ChIP, WB to detect Histone H3 also known as Histone H3.
Quality
Routinely evaluated by western blot analysis.
Western Blot Analysis:
1:2,000-1:20,000 dilution of this lot detected Histone H3 in a modification independent manner in acid extracted proteins from untreated, sodium butyrate or colcemid treated HeLa cells.
Western Blot Analysis:
1:2,000-1:20,000 dilution of this lot detected Histone H3 in a modification independent manner in acid extracted proteins from untreated, sodium butyrate or colcemid treated HeLa cells.
Target description
17 kDa
Physical form
Format: Purified
Purified rabbit monoclonal IgG in buffer containing 0.014 M phosphate buffer, pH 7.6, 0.175 M NaCl, 0.07% sodium azide and 30% glycerol.
Storage and Stability
Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations:
Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol-containing solutions to become frozen during storage.
Handling Recommendations:
Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol-containing solutions to become frozen during storage.
Analysis Note
Control
Acid extracted proteins from HeLa cells, HeLa nuclear extracts or acid extracted HeLa cells treated with sodium butyrate.
Acid extracted proteins from HeLa cells, HeLa nuclear extracts or acid extracted HeLa cells treated with sodium butyrate.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Vanagas, L; Dalmasso, MC; Dubremetz, JF; Portiansky, EL; Olins, DE; Angel, SO
Parasitoloty null
Soraya Bravo et al.
Molecular therapy : the journal of the American Society of Gene Therapy, 21(7), 1403-1412 (2013-05-29)
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Kelby O Kizer et al.
Methods (San Diego, Calif.), 40(4), 296-302 (2006-11-15)
The continuing identification of new histone post-translational modifications and ongoing discovery of their roles in nuclear processes has increased the demand for quick, efficient, and precise methods for their analysis. In the budding yeast Saccharomyces cerevisiae, a variety of methods
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