Recombinant Human Membrane Primary Amine Oxidase/AOC3(C-6His)

Source: Human cells. MW :82.6kD. Recombinant Human Membrane Primary Amine Oxidase is produced by our Mammalian expression system and the target gene encoding Arg27-Asn763 is expressed with a 6His tag at the C-terminus. Vascular adhesion protein-1(VAP-1) 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. 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. VAP-1 vascular expression is regulated at sites of inflammation through its release from intracellular granules in which the protein is stored. 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. VAP-1 mediated adhesion is involved in the process of leukocyte extravasation, an important feature of inflammatory responses. VAP-1 is considered to be a therapeutic target for diabetes, oxidative stress, and inflammatory diseases. Protein function: Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis. [The UniProt Consortium]