NQO1 Antibody [C17H19] | Primary Antibodies

Application: Reactivity: Human

Lane 1: HepG2

Usage Information

Dilution
WB1:2000 IHC1:20000 IF1:400 FCM1:2000

Application
WB, IHC, IF, FCM

Reactivity
Human

Source
Mouse Monoclonal Antibody

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
31 kDa 30 kDa, 31 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human pancreas adenocarcinoma; Human breast adenocarcinoma; Human breast cancer tissue; Dog skin tissue; HeLa cells; HepG2 cells
Negative Control	Human pancreas

Datasheet & SDS

Biological Description

Specificity
NQO1 Antibody [C17H19] detects endogenous levels of total NQO1 protein.

Clone
C17H19

Synonym(s)
DIA4; NMOR1; NQO1; NAD(P)H dehydrogenase [quinone] 1; Azoreductase; DT-diaphorase; Menadione reductase; NAD(P)H:quinone oxidoreductase 1; Phylloquinone reductase; Quinone reductase 1; DTD; QR1

Background
NQO1 (NAD(P)H:quinone oxidoreductase 1) is a cytosolic, FAD-dependent flavoprotein and member of the NAD(P)H dehydrogenase family that catalyzes obligatory two-electron reduction of quinones to stable hydroquinones using NADH or NADPH, thereby preventing redox cycling and oxidative stress. Regulated by the Nrf2/ARE pathway, NQO1 serves as a key cytoprotectant, but is absent in approximately 20–35% of individuals due to a C609T polymorphism that abolishes its stability. NQO1 functions as a homodimer with intersubunit active sites, each monomer binding a tightly associated FAD cofactor and featuring a Tyr128/His161 catalytic dyad that facilitates hydride transfer. Operating via ping-pong kinetics, NQO1 first uses NAD(P)H to reduce FAD, after which oxidized NAD(P)+ exits and the quinone substrate binds for two-electron reduction; dicoumarol acts as a competitive inhibitor at the quinone site. NQO1 detoxifies quinones and xenobiotics by bypassing the formation of semiquinone radicals that would result from one-electron reduction by CYP450OR, stabilizes p53 to promote DNA repair and apoptosis, maintains plasma membrane ubiquinone for plasma membrane electron transport (PMET) and redox homeostasis, directly scavenges superoxide, and regulates proteasome-mediated degradation of proteins such as HIF1α. Oxidative stress leads to Keap1-mediated release of Nrf2, which upregulates NQO1 expression via antioxidant response elements (AREs); post-translationally, NQO1 binds the 20S proteasome to protect substrates during electrophile exposure. Loss of NQO1 heightens ROS and H2O2 levels, resulting in myeloid hyperplasia, benzene toxicity, and reduced apoptosis in knockout models.

Background

NQO1 (NAD(P)H:quinone oxidoreductase 1) is a cytosolic, FAD-dependent flavoprotein and member of the NAD(P)H dehydrogenase family that catalyzes obligatory two-electron reduction of quinones to stable hydroquinones using NADH or NADPH, thereby preventing redox cycling and oxidative stress. Regulated by the Nrf2/ARE pathway, NQO1 serves as a key cytoprotectant, but is absent in approximately 20–35% of individuals due to a C609T polymorphism that abolishes its stability. NQO1 functions as a homodimer with intersubunit active sites, each monomer binding a tightly associated FAD cofactor and featuring a Tyr128/His161 catalytic dyad that facilitates hydride transfer. Operating via ping-pong kinetics, NQO1 first uses NAD(P)H to reduce FAD, after which oxidized NAD(P)+ exits and the quinone substrate binds for two-electron reduction; dicoumarol acts as a competitive inhibitor at the quinone site. NQO1 detoxifies quinones and xenobiotics by bypassing the formation of semiquinone radicals that would result from one-electron reduction by CYP450OR, stabilizes p53 to promote DNA repair and apoptosis, maintains plasma membrane ubiquinone for plasma membrane electron transport (PMET) and redox homeostasis, directly scavenges superoxide, and regulates proteasome-mediated degradation of proteins such as HIF1α. Oxidative stress leads to Keap1-mediated release of Nrf2, which upregulates NQO1 expression via antioxidant response elements (AREs); post-translationally, NQO1 binds the 20S proteasome to protect substrates during electrophile exposure. Loss of NQO1 heightens ROS and H2O2 levels, resulting in myeloid hyperplasia, benzene toxicity, and reduced apoptosis in knockout models.

References
https://pubmed.ncbi.nlm.nih.gov/20361926/ https://pubmed.ncbi.nlm.nih.gov/16700548/

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

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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%