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SAB4200193

Sigma-Aldrich

Anti-Glyoxalase I antibody, Rat monoclonal

clone Clone 6F10, purified from hybridoma cell culture

Sinonimo/i:

Monoclonal Anti-Glyoxalase I antibody produced in rat

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rat

Coniugato

unconjugated

Forma dell’anticorpo

purified from hybridoma cell culture

Tipo di anticorpo

primary antibodies

Clone

Clone 6F10, monoclonal

Forma fisica

buffered aqueous solution

PM

~21 kDa

Reattività contro le specie

mouse, monkey, canine, rat, human

Confezionamento

antibody small pack of 25 μL

Concentrazione

~1.0 mg/mL

tecniche

immunocytochemistry: suitable
western blot: 0.12-0.25 μg/mL using A549, HeLa, SH-SY5Y, COS7 or MDCK cell extracts

Isotipo

IgG2b

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... GLO1(2739)
mouse ... Glo1(109801)
rat ... Glo1(294320)

Descrizione generale

Monoclonal Anti-Glyoxalase I (rat IgG2b isotype) is derived from the hybridoma 6F10 produced by the fusion of mouse myeloma cells and splenocytes from rat immunized with a mouse Glyoxalase I fusion protein. The glyoxalase system, which consists of glyoxalase I (GLO1), glyoxalase II, and a catalytic amount of reduced glutathione (GSH), is important part of cellular metabolism. GLO1 appears to be ubiquitously expressed in all mammalian cells, suggesting its biological importance.

Immunogeno

mouse Glyoxalase I fusion protein

Applicazioni

Monoclonal Anti-Glyoxalase I antibody produced in rat has been used in immunoblotting. and immunocytochemistry.

Azioni biochim/fisiol

The glyoxalase system plays a major role to detoxify α-ketoaldehydes, especially methylglyoxal (MG), that are endogenously formed as a by-product of the triosephosphate isomerase reaction during glycolysis. A member of this system, GLO1 catalyzes the isomerization of a hemithioacetal, comprised of a nonenzymatic adduct of MG and glutathione (GSH), to the corresponding α-d-hydroxyacid thioester and S-D-lactoylglutathione. Studies have suggested that GLO1 may be important for brain function since, GLO1 in the brain is involved in Alzheimer′s disease, autism, anxiety and the regulation of theta oscillations during sleep.

Stato fisico

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

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

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Yusuke Nakadate et al.
Hybridoma (2005), 28(6), 447-450 (2009-12-23)
Glyoxalase I (GLO1) is a key enzyme that plays a role in the detoxification of methylglyoxal (MG), a toxic cellular metabolite produced during glycolysis. The present study reports on the preparation and properties of a monoclonal antibody (MAb) directed against
Tumor necrosis factor-induced modulation of glyoxalase I activities through phosphorylation by PKA results in cell death and is accompanied by the formation of a specific methylglyoxal-derived AGE
Van Herreweghe F, et al.
Proceedings of the National Academy of Sciences of the USA, 99(2), 949-954 (2002)
Glyoxalase 1 and glutathione reductase 1 regulate anxiety in mice
Hovatta I, et al
Nature, 438(7068), 662-662 (2005)
Deleterious Effect of Advanced CKD on Glyoxalase System Activity not Limited to Diabetes Aetiology
Pacal L, et al.
International Journal of Molecular Sciences, 19(5), 1517-1517 (2018)
Methylglyoxal: an emerging signaling molecule in plant abiotic stress responses and tolerance
Hoque TS, et al.
Frontiers in Plant Science, 7(20), 1341-1341 (2016)

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