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Key Documents

SAB4500352

Sigma-Aldrich

Anti-Histone H3 antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

H3/a, H3/c, H3/d, H3/f, H3/h

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About This Item

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 15 kDa

Espèces réactives

human, rat, mouse

Concentration

~1 mg/mL

Technique(s)

ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

Numéro d'accès NCBI

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... HIST1H3A(8350)

Description générale

Anti-Histone H3 Antibody detects endogenous levels of total Histone H3 protein.
Mammals contain three main classes of histone H3 variants: the replicative histones (H3.1 and H3.2), the replacement histone (H3.3) and the centromeric histone (Cenp-A). Histone H3 is located on human chromosome 6p22.

Immunogène

The antiserum was produced against synthesized peptide derived from human Histone H3.

Immunogen Range: 1-50

Application

Anti-Histone H3, N-Terminal antibody has been used in western blotting and enzyme-linked immunosorbent assay (ELISA).

Actions biochimiques/physiologiques

Histone proteins are basic building blocks of chromatin. Histone H3 K27M mutations in adult cerebellar high-grade gliomas. It controls protein-protein interactions to induce binding of trans-acting factors that “drive” chromatin condensation.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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

Histone Demethylation and Toll?like Receptor 8?Dependent Cross?Talk in Monocytes Promotes Transdifferentiation of Fibroblasts in Systemic Sclerosis Via Fra?2.
Ciechomska M, et al.
Arthritis and Rheumatism, 68(6), 1493-1504 (2016)
Dihydromyricetin protects against liver ischemia/reperfusion induced apoptosis via activation of FOXO3a-mediated autophagy.
Chen Y, et al.
Oncotarget, 7(47), 76508-76508 (2016)
Yongbiao Chen et al.
Oncotarget, 7(47), 76508-76522 (2016-10-30)
Liver ischemia and reperfusion (I/R) injury is characterized by defective liver autophagy accompanied by alterations to the endogenous defense system. Dihydromyricetin (DHM) is a natural flavonoid that demonstrates a wide range of physiological functions, and has been implicated as a
Parissa C Monem et al.
PLoS genetics, 19(1), e1010577-e1010577 (2023-01-11)
As ribosomes translate the genetic code, they can encounter a variety of obstacles that hinder their progress. If ribosomes stall for prolonged times, cells suffer due to the loss of translating ribosomes and the accumulation of aberrant protein products. Thus
Omar Ramírez-Nuñez et al.
Journal of neurochemistry, 158(2), 482-499 (2021-04-28)
Nucleocytosolic transport, a membrane process, is impaired in motor neurons in amyotrophic lateral sclerosis (ALS). This study analyzes the nuclear lipidome in motor neurons in ALS and examines molecular pathways linked to the major lipid alterations. Nuclei were obtained from

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