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Glucose 6 Phosphate Dehydrogenase Rabbit mAb

Catalog No.: F4025

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IP1:40 IHC1:2000 IF1:100 FCM1:400

Application
WB, IP, IHC, IF, FCM

Reactivity
Mouse, Rat, Human

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
59 kDa 59 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
Glucose 6 Phosphate Dehydrogenase Rabbit mAb detects endogenous levels of total Glucose 6 Phosphate Dehydrogenase protein.

Clone
N10E9

Synonym(s)
Glucose-6-phosphate 1-dehydrogenase, G6PD

Background
Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway (PPP) and plays a fundamental role in cellular redox balance. Its primary physiological function is to generate nicotinamide adenine dinucleotide phosphate (NADPH), which provides reducing power to specific cells, particularly erythrocytes, thereby protecting them from oxidative damage. By sustaining the intracellular NADPH pool, G6PD is essential for redox homeostasis in healthy individuals. Functioning as a classical oxidoreductase, G6PD activity is tightly regulated by post-translational modifications. Acetylation at Lys-403 by ELP3 suppresses its activity by preventing homodimerization, whereas deacetylation at the same site by SIRT2 enhances enzymatic function. The enzyme catalyzes the oxidative conversion of D-glucose-6-phosphate to D-ribulose-5-phosphate, a key step in the PPP. Mutations in the G6PD gene at various positions can impair substrate binding, reducing production of D-ribulose-5-phosphate and overall enzyme efficiency. G6PD is also highly susceptible to phosphorylation, which is thought to contribute significantly to loss of activity and the onset of hemolytic anemia. Deficiency in G6PD disrupts redox equilibrium, leading to impaired cell signaling, abnormal cell growth, developmental defects, and altered susceptibility to infections. Although ubiquitously expressed with a housekeeping role across tissues, G6PD is particularly vital for the structural integrity and survival of red blood cells, which rely heavily on NADPH for protection against oxidative stress.

Background

Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway (PPP) and plays a fundamental role in cellular redox balance. Its primary physiological function is to generate nicotinamide adenine dinucleotide phosphate (NADPH), which provides reducing power to specific cells, particularly erythrocytes, thereby protecting them from oxidative damage. By sustaining the intracellular NADPH pool, G6PD is essential for redox homeostasis in healthy individuals. Functioning as a classical oxidoreductase, G6PD activity is tightly regulated by post-translational modifications. Acetylation at Lys-403 by ELP3 suppresses its activity by preventing homodimerization, whereas deacetylation at the same site by SIRT2 enhances enzymatic function. The enzyme catalyzes the oxidative conversion of D-glucose-6-phosphate to D-ribulose-5-phosphate, a key step in the PPP. Mutations in the G6PD gene at various positions can impair substrate binding, reducing production of D-ribulose-5-phosphate and overall enzyme efficiency. G6PD is also highly susceptible to phosphorylation, which is thought to contribute significantly to loss of activity and the onset of hemolytic anemia. Deficiency in G6PD disrupts redox equilibrium, leading to impaired cell signaling, abnormal cell growth, developmental defects, and altered susceptibility to infections. Although ubiquitously expressed with a housekeeping role across tissues, G6PD is particularly vital for the structural integrity and survival of red blood cells, which rely heavily on NADPH for protection against oxidative stress.

References
https://pubmed.ncbi.nlm.nih.gov/30258923/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%