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ALOXE3 is a member of the lipoxygenase family, which are catabolized by arachidonic acid-derived compounds. Additionally we are shipping ALOXE3 Antibodies (53) and ALOXE3 Kits (11) and many more products for this protein.
Showing 3 out of 4 products:
Case Report: homozygous ALOXE3 mutation causing autosomal recessive congenital ichthyosis (show LBR Proteins).
Loss-of-function mutations in the LOX (show LOX Proteins) genes ALOX12B (show ALOX12B Proteins) and ALOXE3 have been found to represent the second most common cause of autosomal recessive congenital ichthyosis (show LBR Proteins). [review]
This review covers the background to discovery of the two key lipoxygenases (LOX (show LOX Proteins)) involved in epidermal barrier function, 12R-LOX (show ALOX12B Proteins) and eLOX3. [review]
Autosomal recessive congenital ichthyosis (show LBR Proteins) patients with NIPAL4 (show NIPAL4 Proteins) mutations and abnormal ichthyin (show NIPAL4 Proteins) expression showed increased 12R-LOX (show ALOX12B Proteins) and eLOX-3 staining and a colocalization signal of these LOXs that was three times the normal intensity.
On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1.
Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids.
ALOX12B (show ALOX12B Proteins) mutations are the leading cause of self-improving collodion ichthyosis (show LBR Proteins) in Scandinavia, followed by ALOXE3 mutations, and TGM1 (show TGM1 Proteins) mutations
Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B (show ALOX12B Proteins)) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1.
eLOX-3 hydrolase functions in the normal process of skin differentiation, and that the loss of function mutations are the basis of the LOX (show LOX Proteins)-dependent form of Non-bullous congenital ichthyosiform erythroderma.
The substrate preference of mouse eLOX3 and the unique occurrence of an 8S-LOX (show ALOX15B Proteins) enzyme in mouse skin point to a potential LOX (show LOX Proteins) pathway for the production of epoxyalcohol in murine epidermal differentiation.
Aloxe3 deficiency in mice resulted in early postnatal death. Skin lipid analysis demonstrated that the severity of barrier failure is related to the loss of covalently bound ceramides in both ALOX12B (show ALOX12B Proteins)- and Aloxe3-null mice.
expression of eLOX3 or addition of eLOX3 products stimulated adipogenesis under conditions that normally require an exogenous PPAR gamma (show PPARG Proteins) ligand for differentiation
The 12R-LOX (show ALOX12B Proteins)-eLOX-3 pathway plays a key role in the process of epidermal barrier acquisition by affecting lipid metabolism, as well as protein processing.
findings suggest that endogenous PPARgamma (show PPARG Proteins) ligand(s) promoting adipocyte differentiation are generated via a baicalein-sensitive pathway involving the novel eLOX-3
This gene is a member of the lipoxygenase family, which are catabolized by arachidonic acid-derived compounds. The encoded enzyme is a hydroperoxide isomerase that synthesizes a unique type of epoxy alcohol (8R-hydroxy-11R,12R-epoxyeicosa-5Z,9E,14Z-trienoic acid) from 12R-hydroperoxyeicosatetraenoic acid (12R-HPETE). This epoxy alcohol can activate the the nuclear receptor peroxisome proliferator-activated receptor alpha (PPARalpha), which is implicated in epidermal differentiation. Loss of function of the enzyme encoded by this gene results in ichthyosis, implicating the function of this gene in the differentiation of human skin. This gene is part of a cluster of lipoxygenase genes on 17p13.1. Mutations in this gene result in nonbullous congenital ichthyosiform erythroderma (NCIE). Multiple transcript variants encoding different isoforms have been found for this gene.
arachidonate lipoxygenase 3
, epidermal lipoxygenase
, epidermis-type lipoxygenase 3
, arachidonate 15-lipoxygenase, type B