LOXL2 Protein, Mouse (HEK293, His)

LOXL2 Protein plays a multifaceted role in cellular processes, mediating the post-translational oxidative deamination of lysine residues on target proteins, leading to the formation of deaminated lysine (allysine). Functioning as a transcription corepressor, LOXL2 specifically mediates the deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a tag associated with epigenetic transcriptional activation. Interestingly, LOXL2 shows no 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 the deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, inducing the release of TAF10 from promoters and inhibiting TFIID-dependent transcription. This process leads to the transcriptional repression of genes crucial for embryonic stem cell pluripotency. LOXL2 is also implicated in epithelial to mesenchymal transition (EMT) by interacting with SNAI1 and participating in the repression of E-cadherin. Moreover, LOXL2 is involved in angiogenesis regulation, likely via collagen IV scaffolding, and acts as a regulator of chondrocyte differentiation, showcasing its diverse and intricate roles in cellular and developmental processes.