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ChIPAb+ Acetyl-Histone H4 (Lys8) - ChIP Validated Antibody and Primer Set
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PRODUCT FAMILY INFORMATION
Histone H4 Antibodies and Proteins
Millipore’s Histone H4 antibodies demonstrate specificity against linker histone H4. See below for H4 Antibodies, ChipAb+ Primer sets, and peptides, based on the expertise of Upstate & Chemicon.
EMD Millipore’s Histone H4 antibody demonstrates specificity against linker histone H4. See below for data and references for EMD Millipore’s Histone H4 antibodies and proteins. All EMD Millipore antibodies and proteins are based on the expertise of Upstate & Chemicon.
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Description:
ChIPAb+ Acetyl-Histone H4 (Lys8) - ChIP Validated Antibody and Primer Set
Trade Name:
Upstate (Millipore)
Product Overview:
All ChIPAb+ antibodies are individually validated for chromatin precipitation, every lot, every time. Each ChIPAb+ antibody set includes control primers (tested every lot by qPCR) to biologically validate your IP results in a locus-specific context. The qPCR protocol and primer sequences are provided, allowing researchers to validate ChIP protocols when using our antibody in their chromatin context. Each set also includes a negative control antibody to ensure specificity of the ChIP reaction.
The ChIPAb+ Acetyl-Histone H4 (Lys8) set includes the Acetyl-Histone H4 (Lys8) antibody, a negative control rabbit serum, and qPCR primers which amplify a 134 bp region of human HSPCA. The Acetyl-Histone H4 (Lys8) and negative controls are supplied in a scalable "per ChIP" reaction size and can be used to functionally validate the precipitation of Acetyl-Histone H4 (Lys8)-associated chromatin.
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Specificity:
Recognizes acetyl-Histone H4 (Lys8).
Molecular Weight:
~11 kDa
Immunogen:
Synthetic peptide corresponding to yeast Histone H4 acetylated at lysine 8.
Modifications:
Acetylation
Background Information:
Histone H4 is one of the 5 main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail H4 is involved with the structure of the nucleosomes of the 'beads on a string' structure.
The N-terminal tail of histone H4 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.
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Species Reactivity:
Human
Yeast (S. cerevisiae)
Species Reactivity Note:
Demonstrated to react with Yeast and human. Broad species cross-reactivity is expected based on 100% sequence homology.
Application Notes:
Chromatin Immunoprecipitation:
Sonicated chromatin prepared from HeLa cells (1 X 106 cell equivalents per IP) were subjected to chromatin immunoprecipitation using either 2 µL of Normal Rabbit Serum or 2 µL of Anti-Acetyl-Histone H4 (Lys8) and the Magna ChIP™ A Kit (Cat. # 17-610).
Successful immunoprecipitation of Acetyl-Histone H4 (Lys8) associated DNA fragments was verified by qPCR using ChIP Primers, human HSPCA for a positive, and known Negative Primers (Martinato, F., et al., 2008) as a negative assay (Please see figures).
Data is presented as percent input of each IP sample relative to input chromatin for each amplicon and ChIP sample as indicated.
Please refer to the EZ-Magna ChIP™ A (Cat. # 17-408) or EZ-ChIP™ (Cat. # 17-371) protocol for experimental details.
Western Blot Analysis:
Representative lot data.
Sodium Butyrate-treated HeLa acid extract was resolved by electrophoresis, transferred to PVDF m |