LOXL2
LOXL2 (lysyl oxidase like 2, also known as WS9-14 or LOR) is a member of the lysyl oxidase family that oxidatively deaminates lysine residues on target proteins. It acts both in the extracellular matrix and in the nucleus, where it influences transcription. Browse Assay Genie's current range of LOXL2 research reagents below, or read on for the biology behind the target.
LOXL2 mediates the post-translational oxidative deamination of lysine residues on target proteins, producing deaminated lysine (allysine). When secreted into the extracellular matrix, it promotes cross-linking of matrix proteins by acting on peptidyl lysine residues in precursors of fibrous collagen and elastin. It is also described as a regulator of sprouting angiogenesis, probably through collagen IV scaffolding, and of chondrocyte differentiation.
Within the cell, LOXL2 acts as a transcription corepressor. It specifically deaminates trimethylated Lys-4 of histone H3 (H3K4me3), a mark of transcriptional activation, but shows no activity against H3K9me3, H3K27me3, H3K4me1 or H3K4me2. It also deaminates methylated TAF10, a TFIID subunit, which releases TAF10 from promoters and represses genes needed for embryonic stem cell pluripotency, including POU5F1/OCT4, NANOG, KLF4 and SOX2. In epithelial to mesenchymal transition (EMT), LOXL2 interacts with SNAI1, which recruits it to pericentromeric regions to oxidise histone H3, repress transcription and release CBX5/HP1A, allowing chromatin reorganisation. LOXL2 also participates in repression of E-cadherin (CDH1), including after hypoxia, and interacts with the endoplasmic reticulum protein HSPA5 to activate the IRE1-XBP1 unfolded protein response. These activities suggest a role in tumour progression.
The LOXL2 gene encodes a member of the lysyl oxidase family, whose prototype is an extracellular copper-dependent amine oxidase that catalyses the first step in collagen and elastin crosslinking. A highly conserved C-terminal sequence appears sufficient for amine oxidase activity, while the poorly conserved N-terminus may confer additional roles in developmental regulation, senescence, tumour suppression, cell growth control and chemotaxis. HGNC places LOXL2 in the scavenger receptor cysteine rich domain containing group as well as the lysyl oxidase family.
LOXL2 cross-links collagen and elastin precursors by deaminating peptidyl lysine, making it central to studies of matrix assembly and connective tissue.
Through SNAI1 interaction and E-cadherin repression, including after hypoxia, LOXL2 is studied in EMT and its link to tumour aggressiveness.
LOXL2 deaminates H3K4me3 and methylated TAF10, offering a route to investigate chromatin reorganisation and transcriptional repression.
LOXL2 regulates sprouting angiogenesis, probably via collagen IV scaffolding, and chondrocyte differentiation, supporting developmental and vascular research.
LOXL2 oxidatively deaminates lysine residues, forming allysine. Extracellularly it cross-links collagen and elastin precursors. In the nucleus it deaminates H3K4me3 and methylated TAF10, repressing transcription, and it contributes to EMT through interaction with SNAI1.
LOXL2 is the HGNC symbol for lysyl oxidase like 2, previously named lysyl oxidase-like 2. Aliases include WS9-14 and LOR. UniProt lists the protein as lysyl oxidase homolog 2, and the enzyme carries the EC number 1.4.3.13.
Mouse and rat both have a Loxl2 ortholog. LOXL2 belongs to the lysyl oxidase family, whose members share a highly conserved C-terminal region linked to amine oxidase activity; check the datasheet of any product for its validated reactivity.
Other lysyl oxidase family members that share the conserved C-terminal catalytic region with LOXL2.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y4K0; product specifications from Assay Genie datasheets.