|Description||VAP-1 is a type II membrane cell adhesion protein belonging to the copper/topaquinone oxidase family. It is primarily expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. VAP-1 can catalyze the oxidative deamination of low molecular weight amines, and plays an important role in the migration of lymphocytes to inflamed tissue. Inhibition of VAP-1 can protect against inflammation related damage to certain injured tissues. Additionally, VAP-1 can function as a significant prognostic marker for certain cancers and cardiovascular diseases. Recombinant VAP-1 is a mixture of monomeric and disulfide linked homodimeric forms of a 737 amino acid polypeptide corresponding to amino acids 27 to 763 of the VAP-1 precursor.|
|BiologicalActivity||Measured by its ability to produce hydrogen peroxide during the oxidation of benzylamine. The specific activity >16 pMoles/min/µg of VAP-1.|
|Authenticity||Verified by N-terminal and Mass Spectrometry analyses (when applicable).|
|Endotoxin||Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg).|
|Protein Content||Verified by UV Spectroscopy and/or SDS-PAGE gel.|
|Precautions||Recombinant Human VAP-1 is for research use only and not for use in diagnostic or therapeutic procedures.|
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