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Histone Cluster 2, H4a (HIST2H4A) (acLys5) antibody

Details for Product No. ABIN649866
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Antigen
Synonyms H1ft, Hist4, Hist4h4, FO108, H4, H4/n, H4F2, H4FN, HIST2H4
Epitope
acLys5
(1), (1)
Reactivity
Human, Rat (Rattus)
(2), (1)
Host
Rabbit
(2)
Clonality
Monoclonal
Application
Western Blotting (WB), Immunohistochemistry (IHC)
(2), (1), (1)
Pubmed 3 references available
Quantity 100 µL
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Catalog No. ABIN649866
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Specificity A synthetic peptide corresponding to residues near the N-terminus of human Histone H4 was used as an immunogen.
Alternative Name Histone-H4
Background Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Acetylation of histone H4 thus appears to play a primary role in the structural changes that mediate enhanced binding of transcription factors to their recognition sites within nucleosomes (3). Histone H4 can be reversibly acetylated at lysine residues 5, 8, 12 and 16. It has been shown that, in H4 from human cells, the four lysine residues are acetylated in a preferred, but not exclusive order, namely lysine 16, followed by 12 and 8, followed by 5 (4).
Molecular Weight 11 kDA
Gene ID 8363, 8362, 8359
UniProt P62805
Research Area Ubiquitin-related antibodies, Signaling, Phospho-specific antibodies, Protein Modifications, Transcription Factors, Chromatin, Cell Structure
Application Notes IHC: = 1:250-500, WB: = 1:10000-50000
Comment

Background: Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Acetylation of histone H4 thus appears to play a primary role in the structural changes that mediate enhanced binding of transcription factors to their recognition sites within nucleosomes (3). Histone H4 can be reversibly acetylated at lysine residues 5, 8, 12 and 16. It has been shown that, in H4 from human cells, the four lysine residues are acetylated in a preferred, but not exclusive order, namely lysine 16, followed by 12 and 8, followed by 5 (4).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Histone-H4 Antibody Acetyl (K5) can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications Vettese-Dadey, Grant, Hebbes et al.: "Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro." in: The EMBO journal, Vol. 15, Issue 10, pp. 2508-18, 1996 (PubMed).

Braunstein, Sobel, Allis et al.: "Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern." in: Molecular and cellular biology, Vol. 16, Issue 8, pp. 4349-56, 1996 (PubMed).

Workman, Kingston: "Alteration of nucleosome structure as a mechanism of transcriptional regulation." in: Annual review of biochemistry, Vol. 67, pp. 545-79, 1998 (PubMed).

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