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Merck
CN

A9521

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

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
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Product Name

Anti-Glucose-6-Phosphate Dehydrogenase (G-6-PDH) antibody produced in rabbit, IgG fraction of antiserum, lyophilized powder

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

yeast

technique(s)

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

shipped in

ambient

storage temp.

2-8°C

target post-translational modification

unmodified

Quality Level

Immunogen

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

Physical form

Lyophilized from 0.01 M phosphate buffered saline.

Preparation Note

Reconstitute with 2mL deionized water.

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.

Biochem/physiol Actions

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.

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.

General description

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.

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Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

常规特殊物品
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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)
Molecular Hematopathology
Hematologic Pathology, 712-760 (2019)
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)
Nadya Morozova et al.
Nature cell biology, 8(11), 1263-1269 (2006-10-17)
Ypt-Rab GTPases are key regulators of the various steps of intracellular trafficking. Guanine nucleotide-exchange factors (GEFs) regulate the conversion of Ypt-Rabs to the GTP-bound state, in which they interact with effectors that mediate all the known aspects of vesicular transport.
Decreased expression of a member of the Rho GTPase family, Cdc42Hs, in cells from Tangier disease-the small G protein may play a role in cholesterol efflux
Hirano K I, et al.
Febs Letters, 484(3), 275-279 (2000)

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