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AOC3

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All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Background

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 Comparative schematic of intracellular and membrane/soluble AOC3 distribution in resting and inflamed blood-brain barrier endothelium. (OA Literature)Fig. 1 Inflammation triggers MMP-dependent shedding of soluble AOC3 from brain endothelial cells to promote leukocyte recruitment across the blood-brain barrier.1

AOC3 Protein Function: Core Roles in Copper-Dependent Amine Oxidation and Leukocyte Trafficking Tuning

The biological functions of AOC3 are focused on copper-catalyzed amine oxidation, leukocyte endothelial adhesion and vascular inflammatory control:

  • Copper-Dependent Amine Catalysis: Oxidizes primary amine substrates to generate bioactive inflammatory aldehyde products.
  • Leukocyte Adhesion Crosslinking: Mediates glycan-dependent tethering of circulating immune cells to vascular endothelium.
  • Basal Vascular Immune Surveillance: Maintains low-level leukocyte recruitment under resting tissue conditions.
  • Inflammatory Trafficking Modulation: Governs the magnitude of leukocyte transendothelial migration upon tissue injury.
  • Disease Relevance: AOC3 loss reduces inflammatory cell infiltration, while overexpression drives sustained vascular inflammation.

AOC3 Protein Product

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.

AOC3 Protein Product

Not finding the membrane protein product you need? Contact us to start your one-stop custom service!

AOC3 Stable Cell Line Product

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.

AOC3 Stable Cell Line Product

Not finding the stable cell line product you need? Contact us to start your one-stop custom service!

AOC3 Recombinant Antibody Product

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.

AOC3 Recombinant Antibody Product

Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!

Product Features

  • Native Copper Oxidase & Adhesive Activity: Preserves intact amine catalytic and leukocyte tethering capacity for vascular inflammation research.
  • AOC Isoform Specificity: Eliminates non-specific cross-recognition of unrelated copper amine oxidase paralogs.
  • Vascular Immunology Compatibility: Optimized reagent series for endothelial leukocyte trafficking and anti-inflammatory vascular therapeutic screening workflows.
  • Comprehensive Customization Support: Facilitates end-to-end development of customized proteins, antibodies and stable cell lines to address membrane copper oxidase research demands.

Custom AOC3 Research Services

Beyond catalog products, Creative Biolabs offers specialized custom services for AOC3 research:

  • Custom AOC3 Protein Production: Tailored expression of mutant and tagged AOC3 constructs for amine substrate and leukocyte binding analysis.
  • Custom Antibody Development: Generation of AOC3-specific antibodies for endothelial membrane immunostaining.
  • Stable Cell Line Engineering: Construction of AOC3-modified cell models for leukocyte trafficking research.
  • Functional Assay Development: Custom design of copper-dependent amine oxidation and leukocyte adhesion detection workflows.

Frequently Asked Questions (FAQ)

  1. What is the primary function of AOC3?

    AOC3 is a copper-containing endothelial membrane oxidase that catalyzes amine oxidation and mediates leukocyte adhesion to drive inflammatory cell recruitment.

  2. Why is AOC3 a significant research target?

    AOC3 links vascular amine metabolism to leukocyte transendothelial migration, a central driver of tissue inflammatory infiltration.

  3. Are Creative Biolabs' AOC3 products suitable for clinical use?

    No, all AOC3 products and services are strictly for research use only, not intended for clinical diagnosis or treatment.

  4. What types of AOC3 products does Creative Biolabs offer?

    Offerings include full-length AOC3 membrane oxidases, isoform-specific detection antibodies and custom stable cell lines for vascular inflammation research.

  5. How are AOC3 proteins validated for activity?

    AOC3 proteins are validated via copper-dependent amine oxidation and leukocyte adhesion dual functional testing.

Reference
  1. Boyer, David S., et al. "Amine oxidase copper-containing 3 (AOC3) inhibition: a potential novel target for the management of diabetic retinopathy." International Journal of Retina and Vitreous 7.1 (2021): 30. Under Open Access license CC BY 4.0, without modification. https://doi.org/10.1186/s40942-021-00288-7
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