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Merck
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Key Documents

HPA007316

Sigma-Aldrich

Anti-GLUL antibody produced in rabbit

enhanced validation

Ab1, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Sinonimo/i:

Anti-GS antibody produced in rabbit, Anti-Glutamate--ammonia ligase antibody produced in rabbit, Anti-Glutamine synthetase antibody produced in rabbit

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About This Item

Codice UNSPSC:
12352203
Numero Human Protein Atlas:
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Nome Commerciale

Prestige Antibodies® Powered by Atlas Antibodies

Forma fisica

buffered aqueous glycerol solution

Reattività contro le specie

human

Convalida avanzata

recombinant expression
Learn more about Antibody Enhanced Validation

tecniche

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500

Sequenza immunogenica

LQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGP

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... GLUL(2752)

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Immunogeno

Glutamine synthetase recombinant protein epitope signature tag (PrEST)

Applicazioni

Anti-GLUL antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

Azioni biochim/fisiol

GLUL (glutamate-ammonia ligase) gene encodes an ATP-dependent enzyme that catalyzes the synthesis of glutamine from glutamate and ammonia (nitrogen source). It is a member of the glutamine synthetase family. It is an essential enzyme in glutamine neogenesis. It functions in detoxification of ammonia and glutamate, acid-base homeostasis, cell signaling, and cell proliferation. It has a role in proliferation of fetal skin fibroblasts. Defects in this gene are associated with congenital glutamine deficiency. Overexpression of this gene has been observed in some primary liver cancer samples.

Caratteristiche e vantaggi

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST70153

Stato fisico

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Note legali

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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

Dispositivi di protezione individuale

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


Certificati d'analisi (COA)

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Hans-Gert Bernstein et al.
Frontiers in cellular neuroscience, 9, 273-273 (2015-09-01)
There is increasing evidence for disturbances within the glutamate system in patients with affective disorders, which involve disruptions of the glutamate-glutamine-cycle. The mainly astroglia-located enzyme glutamine synthetase (GS) catalyzes the ATP-dependent condensation of ammonia and glutamate to form glutamine, thus
Jong-Ho Choi et al.
Journal of cellular biochemistry, 114(2), 303-313 (2012-08-30)
In our previous study, we screened and isolated genes that were up-regulated after partial pancreatectomy using transcriptomic analysis and glutamate-ammonia ligase (GLUL) was selected for further study based on its effect on differentiation and proliferation. In the immunohistochemical analysis, GLUL
Shojiro Kitajima et al.
Oncotarget, 8(70), 114481-114494 (2018-02-01)
Ammonia is a toxic by-product of metabolism that causes cellular stresses. Although a number of proteins are involved in adaptive stress response, specific factors that counteract ammonia-induced cellular stress and regulate cell metabolism to survive against its toxicity have yet
Ying-Hui Ko et al.
Cancer biology & therapy, 12(12), 1085-1097 (2012-01-13)
Glutamine metabolism is crucial for cancer cell growth via the generation of intermediate molecules in the tricarboxylic acid (TCA) cycle, antioxidants and ammonia. The goal of the current study was to evaluate the effects of glutamine on metabolism in the
Johannes Häberle et al.
The New England journal of medicine, 353(18), 1926-1933 (2005-11-04)
Glutamine synthetase plays a major role in ammonia detoxification, interorgan nitrogen flux, acid-base homeostasis, and cell signaling. We report on two unrelated newborns who had congenital human glutamine synthetase deficiency with severe brain malformations resulting in multiorgan failure and neonatal

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