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05-858R

Sigma-Aldrich

Anti-Histone H4 Antibody, pan, clone 62-10C-2, rabbit monoclonal

clone 62-10C-2, from rabbit

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Synonym(s):
H4, Histone H4, H4 histone family, member A, histone 1, H4a, histone cluster 1, H4a
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

culture supernatant

antibody product type

primary antibodies

clone

62-10C-2, monoclonal

species reactivity

human

technique(s)

western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... H4C1(8359)

General description

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.

Specificity

Broad species cross-reactivity expected based on 100% sequence homology to multiple species.

Immunogen

Epitope: Epitope mapped to residues 25-28.
KLH-conjugated, synthetic peptide corresponding to amino acids 17-28 of Histone H4.

Application

Use Anti-Histone H4 Antibody, pan, clone 62-10C-2 (Rabbit Monoclonal Antibody) validated in WB to detect Histone H4 also known as Histone H4.

Quality

Evaluated by Western Blot in HeLa acid extracts.

Western Blot Analysis: 0.1 µg/ml of this antibody detected histone H4 in 10 µg of HeLa cell lysate.

Target description

10 kDa Observed

Physical form

Format: Purified
Purified Rabbit Monoclonal IgG Supernatant in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl), containing 40% glycerol with 0.05% sodium azide

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Sama F Sleiman et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(43), 14328-14337 (2014-10-24)
Histone deacetylase (HDAC) inhibition improves function and extends survival in rodent models of a host of neurological conditions, including stroke, and neurodegenerative diseases. Our understanding, however, of the contribution of individual HDAC isoforms to neuronal death is limited. In this
Manti Guha et al.
PloS one, 13(11), e0206897-e0206897 (2018-11-15)
Telomeres protect against chromosomal damage. Accelerated telomere loss has been associated with premature aging syndromes such as Werner's syndrome and Dyskeratosis Congenita, while, progressive telomere loss activates a DNA damage response leading to chromosomal instability, typically observed in cancer cells
Saravanan S Karuppagounder et al.
Science translational medicine, 8(328), 328ra29-328ra29 (2016-03-05)
Disability or death due to intracerebral hemorrhage (ICH) is attributed to blood lysis, liberation of iron, and consequent oxidative stress. Iron chelators bind to free iron and prevent neuronal death induced by oxidative stress and disability due to ICH, but
Benjamin E L Lauffer et al.
The Journal of biological chemistry, 288(37), 26926-26943 (2013-07-31)
Histone deacetylases (HDACs) are critical in the control of gene expression, and dysregulation of their activity has been implicated in a broad range of diseases, including cancer, cardiovascular, and neurological diseases. HDAC inhibitors (HDACi) employing different zinc chelating functionalities such

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