LOXL2 Protein, Human (CHO, His)

The LOXL2 protein functions as a mediator in the post-translational oxidative deamination of lysine residues on target proteins, leading to the formation of deaminated lysine (allysine). Acting as a transcription corepressor, LOXL2 specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Notably, LOXL2 does not exhibit activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Additionally, LOXL2 mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, inducing the release of TAF10 from promoters and leading to the inhibition of TFIID-dependent transcription. This repression results in the downregulation of genes essential for embryonic stem cell pluripotency, including POU5F1/OCT4, NANOG, KLF4, and SOX2. LOXL2 is involved in epithelial to mesenchymal transition (EMT), participating in the repression of E-cadherin (CDH1) through the deamination of histone H3. It interacts with the endoplasmic reticulum protein HSPA5, activating the IRE1-XBP1 pathway of the unfolded protein response, and is implicated in E-cadherin repression following hypoxia, potentially contributing to tumor progression. Furthermore, when secreted into the extracellular matrix, LOXL2 promotes the cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. It also acts as a regulator of sprouting angiogenesis and chondrocyte differentiation.