AOC1 Human
HEK293 Cells.
Amiloride-sensitive amine oxidase (copper-containing), DAO, Diamine oxidase, Amiloride-binding protein 1, Amine oxidase copper domain-containing protein 1, Histaminase, Kidney amine oxidase, KAO, ABP, ABP1, DAO1
Greater than 90.0% as determined by SDS-PAGE.
Description
AOC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-751 a.a) containing a total of 738 amino acids, having a molecular mass of 84.2kDa.
AOC1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Product Specs
Amine Oxidase Copper Containing 1, also known as AOC1, is an enzyme classified under the copper-containing amine oxidase protein family. It plays a crucial role in the oxidation of various biogenic amines, encompassing neurotransmitters, xenobiotic amines, and histamine. Deficiencies in AOC1 have been linked to conditions such as dietary histamine intolerance and histaminosis. Moreover, this enzyme has been implicated in tumor progression by promoting AKT signaling and epithelial-mesenchymal transition (EMT) in stomach cancer.
Recombinant human AOC1, expressed in HEK cells, is a single, glycosylated polypeptide chain with a molecular weight of 84.2 kDa. It encompasses amino acids 20 to 751, totaling 738 amino acids. The protein includes a 6-amino acid His-tag fused at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
The AOC1 solution is provided at a concentration of 0.25 mg/ml and is formulated in a buffer consisting of 10% glycerol and Phosphate-Buffered Saline (PBS) at a pH of 7.4.
The purity of AOC1 is determined to be greater than 90% using SDS-PAGE analysis.
Amiloride-sensitive amine oxidase (copper-containing), DAO, Diamine oxidase, Amiloride-binding protein 1, Amine oxidase copper domain-containing protein 1, Histaminase, Kidney amine oxidase, KAO, ABP, ABP1, DAO1
HEK293 Cells.
EPSPGTLPRK AGVFSDLSNQ ELKAVHSFLW SKKELRLQPS STTTMAKNTV FLIEMLLPKK YHVLRFLDKG ERHPVREARA VIFFGDQEHP NVTEFAVGPL PGPCYMRALS PRPGYQSSWA SRPISTAEYA LLYHTLQEAT KPLHQFFLNT TGFSFQDCHD RCLAFTDVAP RGVASGQRRS WLIIQRYVEG YFLHPTGLEL LVDHGSTDAG HWAVEQVWYN GKFYGSPEEL ARKYADGEVD VVVLEDPLPG GKGHDSTEEP PLFSSHKPRG DFPSPIHVSG PRLVQPHGPR FRLEGNAVLY GGWSFAFRLR SSSGLQVLNV HFGGERIAYE VSVQEAVALY GGHTPAGMQT KYLDVGWGLG SVTHELAPGI DCPETATFLD TFHYYDADDP VHYPRALCLF EMPTGVPLRR HFNSNFKGGF NFYAGLKGQV LVLRTTSTVY NYDYIWDFIF YPNGVMEAKM HATGYVHATF YTPEGLRHGT RLHTHLIGNI HTHLVHYRVD LDVAGTKNSF QTLQMKLENI TNPWSPRHRV VQPTLEQTQY SWERQAAFRF KRKLPKYLLF TSPQENPWGH KRTYRLQIHS MADQVLPPGW QEEQAITWAR YPLAVTKYRE SELCSSSIYH QNDPWHPPVV FEQFLHNNEN IENEDLVAWV TVGFLHIPHS EDIPNTATPG NSVGFLLRPF NFFPEDPSLA SRDTVIVWPR DNGPNYVQRW IPEDRDCSMP PPFSYNGTYR PVHHHHHH
Product Science Overview
AOC1 is characterized by its requirement for a copper ion per subunit and the cofactor topaquinone for its enzymatic activity . The enzyme catalyzes the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide. The general reaction can be summarized as follows:
This reaction is crucial for the metabolism of amino groups and is involved in several metabolic pathways, including the urea cycle, histidine metabolism, and phenylalanine metabolism .
The enzyme’s ability to degrade histamine makes it a target for drug design, particularly in the treatment of inflammatory diseases and conditions related to histamine intolerance . Additionally, the structural information available for AOC1 has facilitated the development of computer-aided inhibitor design, which aims to create specific inhibitors that can modulate the enzyme’s activity without causing adverse effects .
Recent studies have focused on understanding the species-specific binding properties of AOC1 and its inhibitors. This research is essential for preclinical testing and the development of effective therapeutic agents . The structural bioinformatics and structural biology approaches applied in these studies provide valuable insights into the enzyme’s function and its interactions with potential inhibitors .
