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Documenti fondamentali

SAB4504020

Sigma-Aldrich

Anti-phospho-ATP-Citrate Lyase (pSer454) antibody produced in rabbit

affinity isolated antibody

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41
Coniugato:
unconjugated
application:
ELISA
IHC
WB
Clone:
polyclonal
Reattività contro le specie:
mouse, rat, human
citations:
8
tecniche:
ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

antigen 120 kDa

Reattività contro le specie

mouse, rat, human

Concentrazione

~1 mg/mL

tecniche

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

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

phosphorylation (pSer454)

Informazioni sul gene

human ... ACLY(47)

Descrizione generale

ATP citrate lyase (ACLY) is encoded by the gene mapped to human chromosome 17q21.2. It is localized in the cytoplasm and is widely expressed in mammalian tissues.. ACLY is a 440 KDa tetrameric protein containing four apparently identical subunits.

Immunogeno

The antiserum was produced against synthesized peptide derived from human ATP-Citrate Lyase around the phosphorylation site of Ser454.

Immunogen Range: 420-469

Applicazioni

Anti-phospho-ATP-Citrate Lyase (pSer454) antibody produced in rabbit has been used in immunohistochemistry.

Azioni biochim/fisiol

ACLY (ATP citrate lyase) is responsible for cleavage of mitochondria-derived citrate to generate oxaloacetic acid (OAA) and acetyl-CoA, which is required for lipid biogenesis. This enzyme couples energy metabolism with fatty acids and facilitates cell growth. In addition, ACLY is also essential for DNA-damage-induced histone acetylation. ACLY is upregulated in several types of cancers and is associated with cancer cell proliferation. Elevated expression of the gene leads to the development of breast cancer. Thus, ACLY -related inhibitors can be considered as a potential strategy for treating breast cancer.

Caratteristiche e vantaggi

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.

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Certificati d'analisi (COA)

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Nuclear Acetyl-CoA Production by ACLY Promotes Homologous Recombination
Sivanand S, et al.
Molecular Cell, 67(2), 252-265 (2017)
ATP Citrate Lyase (ACLY): A Promising Target for Cancer Prevention and Treatment
Khwairakpam D, et al.
Current Drug Targets, 16(2), 156-163 (2015)
ATP citrate lyase is increased in human breast cancer, depletion of which promotes apoptosis.
Wang D, et al.
Tumour Biology : the Journal of the International Society For Oncodevelopmental Biology and Medicine, 39(4), 1010428317698338-1010428317698338 (2017)
Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age
Elshourbagy N A, et al.
The Journal of Biological Chemistry, 265(3), 1430-1435 (1990)
Sharanya Sivanand et al.
Molecular cell, 67(2), 252-265 (2017-07-12)
While maintaining the integrity of the genome and sustaining bioenergetics are both fundamental functions of the cell, potential crosstalk between metabolic and DNA repair pathways is poorly understood. Since histone acetylation plays important roles in DNA repair and is sensitive

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