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Merck

SAB4200193

Sigma-Aldrich

Anti-Glyoxalase I antibody, Rat monoclonal

clone Clone 6F10, purified from hybridoma cell culture

Synonym(e):

Monoclonal Anti-Glyoxalase I antibody produced in rat

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rat

Konjugat

unconjugated

Antikörperform

purified from hybridoma cell culture

Antikörper-Produkttyp

primary antibodies

Klon

Clone 6F10, monoclonal

Form

buffered aqueous solution

Mol-Gew.

~21 kDa

Speziesreaktivität

mouse, monkey, canine, rat, human

Verpackung

antibody small pack of 25 μL

Konzentration

~1.0 mg/mL

Methode(n)

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

Isotyp

IgG2b

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Immunogen

mouse Glyoxalase I fusion protein

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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)
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
Glyoxalase 1 and glutathione reductase 1 regulate anxiety in mice
Hovatta I, et al
Nature, 438(7068), 662-662 (2005)
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)
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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