ALOXE3 Knockout Cell Line (HEK293)

The choice depends on whether you are studying ALOXE3 (epidermal-type lipoxygenase 3, eLOX-3)'s role as a hepoxilin-generating epidermal lipoxygenase or modeling autosomal recessive congenital ichthyosis (ARCI). The Knockout line is the standard tool for asking whether ALOXE3 is required for these processes — ALOXE3 is an atypical lipoxygenase that lacks dioxygenase activity but converts 12R-HPETE (the product of ALOX12B) into hepoxilin A3 (8R-hydroxy-11R,12R-epoxy-eicosatrienoic acid) and related epidermal lipid signaling molecules essential for proper skin barrier formation. Overexpression is useful for studying ALOXE3 gain-of-function effects. For skin biology research, the EDITGENE ALOXE3 Knockout in HEK293 is highly relevant — ALOXE3 biallelic loss-of-function mutations cause ⭐ autosomal recessive congenital ichthyosis (ARCI), a severe skin barrier disorder. This product complements the parallel ALOX12B Knockout in HEK293 (also available) for studying the ALOX12B-ALOXE3 epidermal lipoxygenase pathway. Rescue with wild-type ALOXE3 enables structure-function studies. The knockout is valuable for studying epidermal lipid biology, hepoxilin signaling, and ichthyosis disease mechanisms.

Primary applications: • Hepoxilin synthesis: hepoxilin A3 and related epidermal lipid analysis by LC-MS. • ARCI modeling: rescue with patient-derived ALOXE3 mutations for autosomal recessive congenital ichthyosis disease modeling. • ALOX12B-ALOXE3 pathway: paired analysis with ALOX12B KO in HEK293 (also available) for complete epidermal lipoxygenase pathway dissection. • Skin barrier biology: in heterologous keratinocyte-relevant contexts, epidermal lipid biosynthesis analysis. EDITGENE recommends this model paired with ALOX12B KO for systematic epidermal lipoxygenase pathway research.

Yes. ALOXE3 rescue experiments are well-established for epidermal lipid research: • Construct design: use a codon-modified ALOXE3 sequence with a small C-terminal tag (FLAG, HA). ALOXE3 has the lipoxygenase architecture but with atypical (lacking standard dioxygenase) activity — preserve protein integrity. • Catalytically-dead rescue: active site iron-binding mutations abolish hepoxilin synthase activity. • ARCI patient mutation rescue: patient-derived ALOXE3 mutations enable disease modeling. • Functional readout: rescue should restore hepoxilin A3 generation from 12R-HPETE substrate. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation.