Recombinant Human Hydroperoxide Isomerase Aloxe3 (ALOXE3) Protein (His)
Beta LifeScience
SKU/CAT #: BLC-00347P

Greater than 90% as determined by SDS-PAGE.
Recombinant Human Hydroperoxide Isomerase Aloxe3 (ALOXE3) Protein (His)
Beta LifeScience
SKU/CAT #: BLC-00347P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Hydroperoxide Isomerase Aloxe3 (ALOXE3) Protein (His) is produced by our E.coli expression system. This is a full length protein. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | Q9BYJ1 |
Target Symbol | ALOXE3 |
Species | Homo sapiens (Human) |
Expression System | E.coli |
Tag | C-6His |
Target Protein Sequence | MAVYRLCVTTGPYLRAGTLDNISVTLVGTCGESPKQRLDRMGRDFAPGSVQKYKVRCTAELGELLLLRVHKERYAFFRKDSWYCSRICVTEPDGSVSHFPCYQWIEGYCTVELRPGTARTICQDSLPLLLDHRTRELRARQECYRWKIYAPGFPCMVDVNSFQEMESDKKFALTKTTTCVDQGDSSGNRYLPGFPMKIDIPSLMYMEPNVRYSATKTISLLFNAIPASLGMKLRGLLDRKGSWKKLDDMQNIFWCHKTFTTKYVTEHWCEDHFFGYQYLNGVNPVMLHCISSLPSKLPVTNDMVAPLLGQDTCLQTELERGNIFLADYWILAEAPTHCLNGRQQYVAAPLCLLWLSPQGALVPLAIQLSQTPGPDSPIFLPTDSEWDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFAMATLRQLPLCHPIYKLLLPHTRYTLQVNTIARATLLNPEGLVDQVTSIGRQGLIYLMSTGLAHFTYTNFCLPDSLRARGVLAIPNYHYRDDGLKIWAAIESFVSEIVGYYYPSDASVQQDSELQAWTGEIFAQAFLGRESSGFPSRLCTPGEMVKFLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGTTTLKTYLDTLPEVNISCNNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRRSIAAFQSRLAQISRDIQERNQGLALPYTYLDPPLIENSVSI |
Expression Range | 1-711aa |
Protein Length | Full Length |
Mol. Weight | 87.4 kDa |
Research Area | Cell Biology |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia. |
Subcellular Location | Cytoplasm. |
Protein Families | Lipoxygenase family |
Database References | |
Associated Diseases | Ichthyosis, congenital, autosomal recessive 3 (ARCI3) |
Tissue Specificity | Predominantly expressed in skin. |
Gene Functions References
- Case Report: ALOXE3 mutation causing congenital ichthyosis and recurrent eczema. PMID: 27868147
- In summary, we have identified three novel sequence variants, one in TGM1 and two in ALOXE3, in three consanguineous families segregating lamellar ichthyosis and congenital ichthyosiform erythroderma types of autosomal recessive congenital ichthyosis. PMID: 26578203
- Case Report: homozygous ALOXE3 mutation causing autosomal recessive congenital ichthyosis. PMID: 25423909
- Loss-of-function mutations in the LOX genes ALOX12B and ALOXE3 have been found to represent the second most common cause of autosomal recessive congenital ichthyosis. [review] PMID: 23954555
- This review covers the background to discovery of the two key lipoxygenases (LOX) involved in epidermal barrier function, 12R-LOX and eLOX3. [review] PMID: 24021977
- Autosomal recessive congenital ichthyosis patients with NIPAL4 mutations and abnormal ichthyin expression showed increased 12R-LOX and eLOX-3 staining and a colocalization signal of these LOXs that was three times the normal intensity. PMID: 22622417
- On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1. PMID: 20923767
- Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids. PMID: 20921226
- ALOX12B mutations are the leading cause of self-improving collodion ichthyosis in Scandinavia, followed by ALOXE3 mutations, and TGM1 mutations PMID: 19890349
- Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1. PMID: 11773004
- eLOX-3 hydrolase functions in the normal process of skin differentiation, and that the loss of function mutations are the basis of the LOX-dependent form of Non-bullous congenital ichthyosiform erythroderma. PMID: 15629692
- The substrate preference of mouse eLOX3 and the unique occurrence of an 8S-LOX enzyme in mouse skin point to a potential LOX pathway for the production of epoxyalcohol in murine epidermal differentiation. PMID: 17045234
- Formation of a ligand for the nuclear receptor PPARalpha may be one possibility by which 12R-LOX and eLOX3 contribute to epidermal differentiation. PMID: 17436029
- mutation hotspots in ALOXE3 and allelic heterogeneity in ALOX12B may have roles in autosomal recessive congenital ichthyosis PMID: 19131948