Datasheet

Biological Description

Specificity	eNOS/NOS Type III Antibody [L17A10] detects endogenous levels of total eNOS/NOS Type III protein.
Background	eNOS/NOS Type III, also known as (Endothelial nitric oxide synthase, NOS3) is a constitutively expressed dimeric enzyme predominantly localized in vascular endothelial cells, where it plays a central role in cardiovascular homeostasis by producing nitric oxide (NO), a potent vasodilator. Structurally, eNOS is composed of an N-terminal oxygenase domain, which binds heme, zinc, tetrahydrobiopterin (BH4), and L-arginine, and a C-terminal reductase domain, which contains binding sites for NADPH, FAD, and FMN, with the two domains connected by a calmodulin-binding region; dimerization and cofactor binding are essential for its catalytic activity. Expression of eNOS, though constitutive, is also found in other cell types such as cardiomyocytes, platelets, and certain neurons, and is tightly regulated at transcriptional, posttranscriptional, and posttranslational levels. Functionally, eNOS synthesizes NO from L-arginine in a calcium/calmodulin-dependent manner, and this NO diffuses into vascular smooth muscle cells to activate soluble guanylate cyclase (sGC), increasing cyclic GMP levels and stimulating protein kinase G (PKG)-mediated phosphorylation events that lower intracellular calcium, promote vasodilation, inhibit platelet aggregation, and thereby maintain vascular tone, blood pressure, and endothelial health.

Specificity

eNOS/NOS Type III Antibody [L17A10] detects endogenous levels of total eNOS/NOS Type III protein.

Background

eNOS/NOS Type III, also known as (Endothelial nitric oxide synthase, NOS3) is a constitutively expressed dimeric enzyme predominantly localized in vascular endothelial cells, where it plays a central role in cardiovascular homeostasis by producing nitric oxide (NO), a potent vasodilator. Structurally, eNOS is composed of an N-terminal oxygenase domain, which binds heme, zinc, tetrahydrobiopterin (BH4), and L-arginine, and a C-terminal reductase domain, which contains binding sites for NADPH, FAD, and FMN, with the two domains connected by a calmodulin-binding region; dimerization and cofactor binding are essential for its catalytic activity. Expression of eNOS, though constitutive, is also found in other cell types such as cardiomyocytes, platelets, and certain neurons, and is tightly regulated at transcriptional, posttranscriptional, and posttranslational levels. Functionally, eNOS synthesizes NO from L-arginine in a calcium/calmodulin-dependent manner, and this NO diffuses into vascular smooth muscle cells to activate soluble guanylate cyclase (sGC), increasing cyclic GMP levels and stimulating protein kinase G (PKG)-mediated phosphorylation events that lower intracellular calcium, promote vasodilation, inhibit platelet aggregation, and thereby maintain vascular tone, blood pressure, and endothelial health.

Usage Information

Application

WB, IF

Dilution

WB

1:2500 - 1:10000

Reactivity

Human

Source

Mouse Monoclonal Antibody

MW

140 kDa

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

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/26428312/

eNOS/NOS Type III Antibody [L17A10]

Biological Description

Usage Information

References

Application Data