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H2A Histone Family, Member V (H2AFV) (N-Term) Peptide

Name

H2A Histone Family, Member V (H2AFV)
Synonyms H2AFV, h2afz, h2afv, MGC133654, LOC685909, H2afv
Binding Site

N-Term
5 references available
Certificates ISO 9001:2008
Catalog no. ABIN695353
Quantity 0.1 mg
Price 49.50 $   Plus shipping costs $45.00
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Immunogen Synthetic peptide
Characteristics Blocking peptide for H2AFV (N-term) antibody ABIN651957
Comments

Background: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene encodes a member of the histone H2A family. Several transcript variants encoding different isoforms, have been identified for this gene.

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Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Restrictions For Research Use only

Publications
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Product El Kharroubi, Piras, Zensen et al.: "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter." in: Molecular and cellular biology, Vol. 18, Issue 5, pp. 2535-44, 1998 (PubMed).

Deng, de la Fuente, Fu et al.: "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones." in: Virology, Vol. 277, Issue 2, pp. 278-95, 2000 (PubMed).

Deng, Wang, de la Fuente et al.: "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA." in: Virology, Vol. 289, Issue 2, pp. 312-26, 2001 (PubMed).

Boyne, Pesavento, Mizzen et al.: "Precise characterization of human histones in the H2A gene family by top down mass spectrometry." in: Journal of proteome research, Vol. 5, Issue 2, pp. 248-53, 2006 (PubMed).

Kim, Sprung, Chen et al.: "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." in: Molecular cell, Vol. 23, Issue 4, pp. 607-18, 2006 (PubMed).