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SAB4200182

Sigma-Aldrich

Anti-Glutathione Reductase antibody, Mouse monoclonal

clone GR6, purified from hybridoma cell culture

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Synonym(s):
Anti-GR, Anti-GSR, Anti-Glutathione-disulfide reductase, Anti-NADPH:oxidized glutathione oxidoreductase
MDL number:
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

GR6, monoclonal

form

buffered aqueous solution

mol wt

antigen ~55 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): suitable
western blot: 2-4 μg/mL using whole extracts of human HepG2 cells.

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GSR(2936)

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SAB4200750SAB4200304SAB4200423
conjugate

unconjugated

conjugate

-

conjugate

unconjugated

conjugate

unconjugated

Gene Information

human ... GSR(2936)

Gene Information

human ... GSN(2934)

Gene Information

human ... ATG7(10533)
mouse ... Atg7(74244)
rat ... Atg7(312647)

Gene Information

human ... SYVN1(84447)

clone

GR6, monoclonal

clone

GS-2C4, monoclonal

clone

ATG7-13, monoclonal

clone

HRD1-5, monoclonal

species reactivity

human

species reactivity

rabbit, canine, human, mouse, monkey

species reactivity

human, mouse, rat

species reactivity

human

antibody form

purified from hybridoma cell culture

antibody form

purified from hybridoma cell culture

antibody form

purified from hybridoma cell culture

antibody form

purified from hybridoma cell culture

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General description

Monoclonal Anti-Glutathione Reductase (mouse IgG1 isotype) is derived from the hybridoma GR6 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a human Glutathione reductase recombinant protein. Glutathione reductase is a homodimeric enzyme containing one FAD molecule and NADPH binding domain per subunit. This gene is located on human chromosome 8p.

Immunogen

mice immunized with a human Glutathione reductase recombinant protein. The corresponding proteins in rat and mouse share 86% and 85% homology, respectively.

Application

Monoclonal Anti-Glutathione Reductase antibody produced in mouse has been used in:
  • immunohistochemical
  • immunofluorescence studies
  • immunoblotting
  • immunoprecipitation

Biochem/physiol Actions

Glutathione reductase (GR) is a ubiquitous flavoenzyme involved in protecting cells from stress. GR catalyses the reduction of oxidized glutathione (GSSG) to glutathione (GSH). It is an essential component of the glutathione redox cycle, which maintains adequate levels of reduced cellular GSH. GSH serves as an antioxidant and also as an electron donor for glutathione peroxidases and a substrate for glutathione-S-transferases.

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.

Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Inherited glutathione reductase deficiency and Plasmodium falciparum malaria?a case study
Gallo V, et al.
Testing, 4(10), e7303-e7303 (2009)
Electrostatic control of the isoalloxazine environment in the two-electron reduced states of yeast glutathione reductase
Picaud T and Desbois A
The Journal of Biological Chemistry, 277(35), 31715-31721 (2002)
Inverted tandem duplication of 8p12-p23. 1 in a child with increased activity of glutathione reductase.
Nevin NC, et al.
Journal of medical Genetics, 27(2), 135-136 (1990)
The effect of glucagon-like peptide-1 in the management of diabetes mellitus: cellular and molecular mechanisms.
Lotfy M, et al.
Cell and Tissue Research, 358(2), 343-358 (2014)

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