AOC3 Human
VAP-1, AOC3, HPAO, VAP1, Membrane primary amine oxidase, Copper amine oxidase, HPAO, Semicarbazidesensitive amine oxidase, SSAO, Vascular adhesion protein 1.
Description
AOC3 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 746 amino acids (27-763 aa) and having a molecular mass of 82.8kDa.
AOC3 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
VAP-1, AOC3, HPAO, VAP1, Membrane primary amine oxidase, Copper amine oxidase, HPAO, Semicarbazidesensitive amine oxidase, SSAO, Vascular adhesion protein 1.
ADPGRGGDGG EPSQLPHCPS VSPSAQPWTH PGQSQLFADL SREELTAVMR FLTQRLGPGL VDAAQARPSD NCVFSVELQL PPKAAALAHL DRGSPPPARE ALAIVFFGRQ PQPNVSELVV GPLPHPSYMR DVTVERHGGP LPYHRRPVLF QEYLDIDQMI FNRELPQASG LLHHCCFYKH RGRNLVTMTT APRGLQSGDR ATWFGLYYNI SGAGFFLHHV GLELLVNHKA LDPARWTIQK VFYQGRYYDS LAQLEAQFEA GLVNVVLIPD NGTGGSWSLK SPVPPGPAPP LQFYPQGPRF SVQGSRVASS LWTFSFGLGA FSGPRIFDVR FQGERLVYEI SLQEALAIYG GNSPAAMTTR YVDGGFGMGK YTTPLTRGVD CPYLATYVDW HFLLESQAPK TIRDAFCVFE QNQGLPLRRH HSDLYSHYFG GLAETVLVVR SMSTLLNYDY VWDTVFHPSG AIEIRFYATG YISSAFLFGA TGKYGNQVSE HTLGTVHTHS AHFKVDLDVA GLENWVWAED MVFVPMAVPW SPEHQLQRLQ VTRKLLEMEE QAAFLVGSAT PRYLYLASNH SNKWGHPRGY RIQMLSFAGE PLPQNSSMAR GFSWERYQLA VTQRKEEEPS SSSVFNQNDP WAPTVDFSDF INNETIAGKD LVAWVTAGFL HIPHAEDIPN TVTVGNGVGF FLRPYNFFDE DPSFYSADSI YFRGDQDAGA CEVNPLACLP QAAACAPDLP AFSHGGFSHN HHHHHH
Product Science Overview
Amine Oxidase Copper Containing 3 (AOC3), also known as semicarbazide-sensitive amine oxidase (SSAO) and vascular adhesion protein 1 (VAP-1), is an enzyme that plays a crucial role in various physiological and pathological processes. This enzyme is part of the copper-containing amine oxidase family, which catalyzes the oxidative deamination of primary amines to aldehydes, ammonia, and hydrogen peroxide .
AOC3 is a membrane-bound enzyme that is predominantly expressed in the endothelial cells of blood vessels. It contains a copper ion at its active site, which is essential for its enzymatic activity. The enzyme facilitates the adhesion of leukocytes to the endothelium, a critical step in the inflammatory response. By oxidizing primary amines, AOC3 generates reactive aldehydes and hydrogen peroxide, which can modulate vascular function and leukocyte behavior .
AOC3 is involved in several physiological processes, including:
- Leukocyte Trafficking: AOC3 mediates the adhesion and transmigration of leukocytes across the endothelium, playing a vital role in immune surveillance and inflammation .
- Vascular Function: The enzyme’s activity influences vascular tone and permeability, contributing to the regulation of blood flow and tissue oxygenation .
- Metabolic Regulation: AOC3 is implicated in the metabolism of biogenic amines, which are important for neurotransmission and other cellular functions .
AOC3 has been associated with various pathological conditions, including:
- Diabetic Retinopathy: AOC3 inhibition has been proposed as a therapeutic strategy for diabetic retinopathy, a microvascular complication of diabetes. By reducing leukocyte recruitment and oxidative stress, AOC3 inhibitors may help preserve vision in patients with this condition .
- Lung Cancer: Research has shown that AOC3 exerts anti-mesenchymal transformation effects and enhances CD4+ T-cell recruitment, which can prolong survival in lung cancer patients. Downregulation of AOC3 has been linked to tumor promotion and progression .
Human recombinant AOC3 is produced using recombinant DNA technology, which involves inserting the gene encoding AOC3 into a suitable expression system, such as bacteria or mammalian cells. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant AOC3 retains the enzymatic activity and functional properties of the native protein, making it a valuable tool for studying the enzyme’s role in health and disease.
