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H7789

Sigma-Aldrich

Anti-acetyl-Histone H1.4 (AcLys26) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-H1 Histone family, member 4, Anti-H1e, Anti-Histone 1, Anti-Histone H1b

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~35 kDa

Espèces réactives

human

Technique(s)

western blot: 0.5-1 μg/mL using acid-extracted fraction of HL60 cells

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

acetylation (Lys26)

Informations sur le gène

human ... HIST1H1E(3008)

Description générale

In mammalian cells, four histone H1 variants (H1.2 to H1.5) are present in all somatic cells, and a fifth (H1.1) is restricted to thymus, testis, and spleen and possibly lymphocytic and neuronal cells. Histone H1.4 is di-methylated or acetylated at Lys26. Lys26 is located within the flexible N-terminal domain of H1.4, just preceding the globular domain.

Immunogène

synthetic acetylated peptide corresponding to amino acids 22-33 (Ac-Lys26) of human histone H1.4.

Application

Anti-acetyl-Histone H1.4 (Ac-Lys26) antibody produced in rabbit is suitable for western blot at a concentration of 0.5-1μg/mL using acid-extracted fraction of HL60 cells.
Anti-acetyl-Histone H1.4 (Ac-Lys26) antibody produced in rabbit has been used in western blotting.

Actions biochimiques/physiologiques

H1.4 at lysine residue 26 represses transcription. Linker histone H1 binds to DNA between nucleosomal core particles and is involved in establishing and maintaining higher order chromatin structures. Histone modifications are thought to play an important role in cancer and disease.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26
Walport LJ, et al.
Febs Letters, 592(19), 3264-3273 (2018)
Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the Jumonji domain-containing JMJD2/KDM4 proteins
Trojer P, et al.
The Journal of Biological Chemistry, 284(13), 8395-8405 (2009)
Anti-correlation between longevity gene SirT1 and Notch signaling in ascending aorta biopsies from patients with bicuspid aortic valve disease
Sciacca S, et al.
Heart and Vessels, 28(2), 268-275 (2013)
S Khochbin
Gene, 271(1), 1-12 (2001-06-19)
Genes encoding linker histone variants have evolved to link their expression to signals controlling the proliferative capacities of cells, i.e. cycling and growth-arrested cells express distinct and specific H1 subtypes. In metazoan, these variants show a tripartite structure, with considerably
Jerome Bonnefont et al.
Neuron, 103(6), 1096-1108 (2019-07-30)
During neurogenesis, progenitors switch from self-renewal to differentiation through the interplay of intrinsic and extrinsic cues, but how these are integrated remains poorly understood. Here, we combine whole-genome transcriptional and epigenetic analyses with in vivo functional studies to demonstrate that Bcl6

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