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FCABS325PE

Sigma-Aldrich

Milli-Mark® Anti-acetyl-Histone H3-PE Antibody

Milli-Mark®, from rabbit

Synonyme(s) :

H3t, H3/t, H3/g, Histone H3.1t

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

PE

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

Tetrahymena sp., human, mouse

Fabricant/nom de marque

Milli-Mark®

Technique(s)

flow cytometry: suitable

Isotype

IgG

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

acetylation (Lys9,Lys14)

Informations sur le gène

human ... H3F3B(3021)

Description générale

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ′beads on a string′ structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into RNA.

Spécificité

Antibody recognizes Tetrahymena acetyl Histone H3
This sequence is highly conserved and predicted to have broad species crossreactivity.

Immunogène

KLH-conjugated peptide corresponding to amino acids 1-20 of Tetrahymena histone H3 (ARTKQTAR[K*]STGG[K*]APRKQLC) where K* is acetylated

Application

This Milli-Mark Anti-acetyl-Histone H3-PE Antibody is validated for use in FC for the detection of acetyl-Histone H3.

Qualité

Evaluated by flow cytometry using HeLa cells

Description de la cible

15.5 kDa Calculated

Forme physique

Purified rabbit polyclonal IgG conjugated to PE in PBS with 0.1% sodium azide and 15 mg/mL BSA

Informations légales

MILLI-MARK is a registered trademark of Merck KGaA, Darmstadt, Germany

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

HIV-1 expression within resting CD4+ T cells after multiple doses of vorinostat.
Archin, NM; Bateson, R; Tripathy, MK; Crooks, AM; Yang, KH; Dahl, NP; Kearney et al.
The Journal of Infectious Diseases null
Adam M Spivak et al.
Retrovirology, 13(1), 88-88 (2016-12-22)
Despite the durable viral suppression afforded by antiretroviral therapy, HIV-1 eradication will require strategies to target latently infected cells that persist in infected individuals. Protein kinase C (PKC) activation is a promising strategy to reactivate latent proviruses and allow for
Addie May I Nesbitt et al.
PloS one, 9(5), e94224-e94224 (2014-05-03)
Genetic, pharmacological, and environmental interventions that alter total levels of histone acetylation in specific brain regions can modulate behaviors and treatment responses. Efforts have been made to identify specific genes that are affected by alterations in total histone acetylation and
Valeria Barili et al.
Nature communications, 11(1), 604-604 (2020-02-01)
Hepatitis C virus infection (HCV) represents a unique model to characterize, from early to late stages of infection, the T cell differentiation process leading to exhaustion of human CD8+ T cells. Here we show that in early HCV infection, exhaustion-committed

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