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SAB4200193

Sigma-Aldrich

Anti-Glyoxalase I antibody, Rat monoclonal

clone Clone 6F10, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-Glyoxalase I antibody produced in rat

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rat

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

Clone 6F10, monoclonal

form

buffered aqueous solution

mol wt

~21 kDa

species reactivity

mouse, monkey, canine, rat, human

packaging

antibody small pack of 25 μL

concentration

~1.0 mg/mL

technique(s)

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

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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