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A9521

Sigma-Aldrich

Anti-Glucose-6-Phosphate Dehydrogenase (G-6-PDH) antibody produced in rabbit

IgG fraction of antiserum, lyophilized powder

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

lyophilized powder

Espèces réactives

yeast

Technique(s)

immunoelectrophoresis: suitable
indirect ELISA: 1:15,000-1:30,000

Conditions d'expédition

ambient

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Description générale

G-6-PDH catalyzes the NADP+(or NAD+)-dependent oxidation of D-glucose-6-phosphate to 6-phospho-D-glucono-1,5-lactone. This reaction is the rate limiting step of the pentose phosphate pathway.
Yeast G-6-PDH is often used as a loading control in several immunoassays.
Glucose-6-phosphate dehydrogenase (G6PD) is a cytosolic enzyme. It synthesizes NADPH (nicotinamide adenine dinucleotide phosphate). The G6PD gene is located on human chromosome X. It spans 18.5 kb and has 13 exons.
The product is specific for G-6-PDH as determined by immunoelectrophoresis. No reaction is observed with other proteins in a crude Baker′s yeast extract.

Immunogène

G-6-PDH from Baker′s yeast S. cerevisiae.

Application

Anti-Glucose-6-Phosphate Dehydrogenase (G-6-PDH) antibody has been used to detect the immunoreactive mass of glyceraldehyde 3-phosphate dehydrogenase (GAPDH). It has also been used in western blotting.
Rabbit Anti-Glucose-6-Phosphate Dehydrogenase (G-6-PDH) antibody has been used for western blot assays. The antibody can also be used for indirect ELISA (1:15,000-1:30,000) and immunoelectrophoresis.
Yeast cell extracts were analyzed by western blot and equal loading was determined by probing with rabbit anti-Glucose-6-Phosphate Dehydrogenase antibody.

Actions biochimiques/physiologiques

NADPH (nicotinamide adenine dinucleotide phosphate), produced by glucose-6-phosphate dehydrogenase (G6PD) is an electron donor molecule, that helps in neutralizing harmful oxidizing agents. Deficiency in G6PD shows symptoms, that includes neonatal jaundice and acute episodic hemolysis. This enzyme guards the red blood cells against oxidative challenges.

Forme physique

Lyophilized from 0.01 M phosphate buffered saline.

Reconstitution

Reconstitute with 2mL deionized water.

Clause de non-responsabilité

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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Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Steven D Cappell et al.
The Journal of biological chemistry, 286(17), 14852-14860 (2011-03-11)
Multiple MAP kinase pathways share components yet initiate distinct biological processes. Signaling fidelity can be maintained by scaffold proteins and restriction of signaling complexes to discreet subcellular locations. For example, the yeast MAP kinase scaffold Ste5 binds to phospholipids produced
Molecular Hematopathology
Hematologic Pathology, 712-760 (2019)
A conserved C-terminal element in the yeast Doa10 and human MARCH6 ubiquitin ligases required for selective substrate degradation
Zattas D, et al.
The Journal of Biological Chemistry, 29(7), jbc-M116 (2016)
Cytochemical flow analysis of intracellular G6 PD and aggregate analysis of mosaic G6 PD expression
Kalnoky M, et al.
European Journal of Haematology, 100(3), 294-303 (2018)
Danazol inhibits aromatase activity of endometriosis-derived stromal cells by a competitive mechanism
Murakami K, et al.
Fertility and Sterility, 86(2), 291-297 (2006)

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