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Key Documents

ABE1348

Sigma-Aldrich

Anti-Histone H2A.Z Antibody (C-term)

from rabbit, purified by affinity chromatography

Sinônimo(s):

Histone H2A.Z, H2A/z

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702

fonte biológica

rabbit

Nível de qualidade

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

purificado por

affinity chromatography

reatividade de espécies

human

técnica(s)

ChIP: suitable (ChIP-seq)
ELISA: suitable
immunocytochemistry: suitable
western blot: suitable

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... H2AFZ(3015)

Descrição geral

H2A.Z, also known as H2AFZ, is a variant of histone H2A that is highly conserved from yeast to humans. Like other histone variants, H2A.Z is encoded by a unique gene, resulting in a slightly divergent type of H2A with specialized functions. H2A.Z is involved in chromatin compaction by stabilizing the histone octamer within the nucleosome. It promotes gene expression through the creation of an open domain of chromatin that is more easily transcribed. H2A.Z is nonrandomly distributed throughout the genome, targeted primarily to pericentric heterochromatin, but excluded from the inactive X chromosome and the nucleolus. H2A.Z is associated with both euchromatin and facultative heterochromatin. DNA methylation can influence chromatin structure and effect gene silencing by excluding H2A.Z, and likewise, H2A.Z protects genes from DNA methylation. Thus, H2A.Z plays a role in regulating heterochromatin silencing and is involved in transcriptional control.

Especificidade

Recognizes histone H2A.Z
wide range expected

Imunogênio

KLH-conjugated linear peptide corresponding to region the near C-terminus of Human Histone H2A.Z.

Aplicação

Chromatin Immunoprecipitation (ChIP): A representative lot of this antibody (1μg per reaction) was used for ChIP using chromatin from HeLa and K562 cells.

ChIP-seq: A representative lot of this antibody (0.5 μg per reaction) was used to immunoprecipitate K562 chromatin for ChIP-seq analysis.

Western Blotting Analysis: A 1:2,000 dilution of a represenative lot of this antibody detected histone H2A.Z in acid extracted HeLa cell lysate.

Immunocytochemistry: A 1:500 dilution from a representative lot detected histone H2A.Z in HeLa cells.
This Anti-Histone H2A.Z Antibody (C-term) is validated for use in Western Blotting and Chromatin Immunoprecipitation (ChIP) and ChIP-seq and Immunocytochemistry and ELISA for the detection of Histone H2A.Z (C-term).

Qualidade

Evaluated by Western Blotting using recombinant histones

Western Blotting Analysis: A 1.5 µg/mL dilution of this antibody detected recombinant Histone H2A.Z, but not histones H1, H2A,H2A.X, H3, or H4.

Descrição-alvo

~16 kDa observed

forma física

Affinity purified rabbit polyclonal in PBS containing 0.05% azide and 0.05% ProClin 300.

Outras notas

Concentration: Please refer to lot specific datasheet.

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Pictogramas

Exclamation mark

Palavra indicadora

Warning

Frases de perigo

Classificações de perigo

Skin Sens. 1

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Gilda Stefanelli et al.
Cell reports, 36(7), 109551-109551 (2021-08-19)
Rapid removal of histone H2A.Z from neuronal chromatin is a key step in learning-induced gene expression and memory formation, but mechanisms underlying learning-induced H2A.Z removal are unclear. Anp32e was recently identified as an H2A.Z-specific histone chaperone that removes H2A.Z from
Guang Yang et al.
Nucleic acids research, 48(6), 3001-3013 (2020-01-23)
Nucleosomal histones are barriers to the DNA repair process particularly at DNA double-strand breaks (DSBs). However, the molecular mechanism by which these histone barriers are removed from the sites of DNA damage remains elusive. Here, we have generated a single

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