Human VAP-1/AOC3 Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: VAP-1/AOC3

Vascular adhesion protein-1 (VAP-1), also called AOC3 (amine oxidase copper-containing 3) or SSAO (semicarbazide-sensitive amine oxidase), is a copper amine oxidase with a topaquinone cofactor. VAP-1 is a Type II integral membrane protein, but a soluble form of the enzyme is present in human serum, and its level increases in diabetes and some inflammatory liver diseases (1, 2). Human and mouse VAP-1 share 83% amino acid sequence identity. VAP-1 catalyzes the oxidative deamination of small primary amines such as methylamine, benzylamine, and aminoacetone in a reaction that produces an aldehyde, ammonia, and H₂O₂ (3). The enzyme is sensitive to inhibition by semicarbazide. VAP-1 expression is highest in the endothelium of lung, heart, and intestine, but low in tissues such as brain, spleen, kidney, and liver (4). VAP-1 vascular expression is regulated at sites of inflammation through its release from intracellular granules in which the protein is stored (5). The adhesive function of VAP-1 has been demonstrated in studies showing that the protein is important for the adherence of certain lymphocyte subtypes to inflamed endothelial tissues (6). VAP-1 mediated adhesion is involved in the process of leukocyte extravasation, an important feature of inflammatory responses. The role of VAP-1 amine oxidase activity in this process is not fully defined, but it appears to be carbohydrate-dependent (7). VAP-1 is considered to be a therapeutic target for diabetes, oxidative stress, and inflammatory diseases (8).

Product Datasheets

Related Research Areas

• Additional Reduction/Oxidation (Redox) Enzymes
• Adhesion Molecules on Endothelial Cells
• Cancer Biomarkers
• Oxidases and Oxygenases
• Oxygenases/Hydroxylases
• Pro-oxidant Molecules
• Redox Enzymes