LOXL2 (human, recombinant)

Lysyl oxidase-like 2 (LOXL2) is a copper-dependent amine oxidase and member of the LOX family. It is composed of four N-terminal scavenger receptor cysteine-rich (SRCR) domains and a conserved C-terminal catalytic domain containing a copper-binding site. LOXL2 is secreted by fibroblasts and reproductive epithelial cells and oxidizes lysines to reactive aldehydes to cross-link extracellular matrix (ECM) proteins, such as collagen or elastin. It has roles in connective tissue development, ECM remodeling, fibrosis, and cancer invasion and metastasis. It also oxidizes dimethylated lysine 4 on histone H3 (H3K4me2) and H3K4me3 and reduces the levels of E-cadherin in vitro. The levels of LOXL2 are increased in the airway epithelium in a mouse model of ovalbumin-induced asthma and in patients with asthma. Hepatocyte levels of LOXL2 are increased in patients with Wilson's disease or primary biliary cirrhosis and in patients infected with hepatitis B or -C. Cayman's LOXL2 (human, recombinant) protein can be used for enzyme activity assays. This protein has a calculated molecular weight of 85.5 kDa and a predicted N-terminus of Gly26 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 110-116 kDa due to glycosylation.Synonyms: Lysyl Oxidase-like Protein 2, Lysyl Oxidase-like 2. Purity: >95% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Active recombinant human C-terminal His-tagged LOXL2 expressed in CHO cells. Amino Acids: 1-774 (full length). MW: 85.5 kDa. Formulation: (Request formulation change), Lyophilized from sterile 20 mM MES, with 50 mM sodium chloride. UniProt Accession No: Q9Y4K0.