Vascular adhesion protein-1 (VAP1) is a copper amine oxidase with a topaquinone cofactor. VAP1 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. VAP1 catalyzes the oxidative deamination of small primary amines such as methylamine, benzylamine, and aminoacetone in a reaction that produces an aldehyde, ammonia, and H2O2. The enzyme is sensitive to inhibition by semicarbazide. VAP1 expression is highest in the endothelium of lung, heart, and intestine, but low in tissues such as brain, spleen, kidney, and liver. VAP1 vascular expression is regulated at sites of inflammation through its release from intracellular granules in which the protein is stored. The adhesive function of VAP1 has been demonstrated in studies showing that the protein is important for the adherence of certain lymphocyte subtypes to inflamed endothelial tissues. VAP1 mediated adhesion is involved in the process of leukocyte extravasation, an important feature of inflammatory responses. The role of VAP1 amine oxidase activity in this process is not fully defined, but it appears to be carbohydrate-dependent. VAP1 is considered to be a therapeutic target for diabetes, oxidative stress, and inflammatory diseases. Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived Gly27-Asn763, with an N-terminal Met and 10-His tag, followed by a Gly-Gly-Gly-Ser-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Ser-Ile-Glu-Gly-Arg linker SDS-PAGE: 80-90kD, reducing conditions Activity: Measured by its ability to produce hydrogen peroxide during the oxidation of benzylamine. Specific Activity: 8 pmoles/min/ug. Endotoxin Level: 1EU/1ug (LAL) Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 6 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
