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Amine oxidase copper containing 3 (AOC3, VAP-1) is a membrane-tethered copper-dependent amine oxidase encoded by AOC3 gene, highly expressed on vascular endothelial cells, localized to plasma membrane and extracellular matrix interfaces. Distinct from soluble amine oxidase paralogs, AOC3 carries dual enzymatic and adhesive functions: its copper-containing catalytic domain deaminates primary amines to generate bioactive aldehyde mediators, while extracellular ectodomains mediate leukocyte adhesion receptor crosslinking to support immune cell recruitment across vessel walls. Under steady vascular conditions, basal AOC3 activity maintains low-level leukocyte surveillance without excessive inflammatory infiltration. Upon inflammatory stimulation, elevated surface AOC3 amplifies amine catabolism and immune cell tethering to drive tissue leukocyte accumulation. Unlike purely catalytic oxidases, AOC3 combines enzymatic signaling and cell adhesion functions that cannot be fully substituted by other copper amine oxidases, linking vascular amine metabolism to leukocyte trafficking pathways. Loss of functional AOC3 weakens inflammatory leukocyte recruitment and reduces tissue inflammatory infiltration, while sustained AOC3 activity amplifies vascular inflammatory responses, establishing AOC3 as a core research target for endothelial membrane enzyme biology and anti-inflammatory vascular modulator screening.
AOC3 executes dual copper-dependent catalytic and adhesive function anchored to endothelial cell surface bilayers, utilizing conserved copper-binding catalytic pockets to mediate amine substrate oxidation and separate extracellular adhesion domains to bind leukocyte surface glycans. Conserved catalytic active sites exclusively target primary amine substrates, separating its enzymatic spectrum from other oxidase family proteins. AOC3-mediated dual activity bridges circulating amine metabolism and leukocyte endothelial tethering, balancing vascular inflammatory infiltration magnitude based on local inflammatory stimulus load. AOC3 participates in post-capillary leukocyte recruitment, vascular inflammatory mediator generation and endothelial immune surveillance. Deficient AOC3 expression disrupts leukocyte transendothelial migration and impairs tissue inflammatory responses. Therefore, AOC3 represents a pivotal research target for copper-containing membrane oxidase study and vascular anti-inflammatorycompound screening.
Fig. 1 Inflammation triggers MMP-dependent shedding of soluble AOC3 from brain endothelial cells to promote leukocyte recruitment across the blood-brain barrier.1
The biological functions of AOC3 are focused on copper-catalyzed amine oxidation, leukocyte endothelial adhesion and vascular inflammatory control:
Creative Biolabs offers high-quality AOC3 proteins through optimized expression systems, including full-length endothelial membrane oxidase and isolated copper catalytic domain variants. These products retain native amine oxidation and leukocyte adhesion dual activity, suitable for enzyme-substrate interaction and vascular inflammatory modulator screening. All AOC3 proteins undergo strict quality control to ensure consistent performance and reliable application across diverse research platforms.
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Creative Biolabs provides custom-engineered AOC3 stable cell lines, including overexpression and blank control models. These cell lines are optimized for membrane oxidase expression profiling and leukocyte trafficking functional analysis. Each cell line undergoes stringent validation to ensure stable expression profiles and consistent functional performance in diverse experimental contexts.
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High-specificity recombinant antibodies targeting AOC3 are developed via advanced antibody engineering technologies, with no cross-reactivity with other copper amine oxidase family proteins. These antibodies are validated for endothelial plasma membrane localization detection and vascular tissue expression profiling, and can be combined with leukocyte adhesion marker reagents to analyze complete AOC3 trafficking complexes in endothelial cell models.
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Beyond catalog products, Creative Biolabs offers specialized custom services for AOC3 research:
AOC3 is a copper-containing endothelial membrane oxidase that catalyzes amine oxidation and mediates leukocyte adhesion to drive inflammatory cell recruitment.
AOC3 links vascular amine metabolism to leukocyte transendothelial migration, a central driver of tissue inflammatory infiltration.
No, all AOC3 products and services are strictly for research use only, not intended for clinical diagnosis or treatment.
Offerings include full-length AOC3 membrane oxidases, isoform-specific detection antibodies and custom stable cell lines for vascular inflammation research.
AOC3 proteins are validated via copper-dependent amine oxidation and leukocyte adhesion dual functional testing.