Description
Recombinant Human ERO1A/ERO1L Protein (His Tag) | PKSH032401 | Gentaur US, UK & Europe Disrtribition
Synonyms: ERO1-Like Protein Alpha; ERO1-L; ERO1-L-Alpha; Endoplasmic Oxidoreductin-1-Like Protein; Oxidoreductin-1-L-Alpha; ERO1L
Active Protein: N/A
Activity: Recombinant Human ERO1-Like Protein alpha is produced by our Mammalian expression system and the target gene encoding Glu24-His468 is expressed with a 6His tag at the C-terminus.
Protein Construction: Recombinant Human ERO1-Like Protein alpha is produced by our Mammalian expression system and the target gene encoding Glu24-His468 is expressed with a 6His tag at the C-terminus.
Fusion Tag: C-6His
Species: Human
Expressed Host: Human Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 53.0 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH7.4.
Reconstitution: Please refer to the printed manual for detailed information.
Background: ERO1-Like Protein α (ERO1L) is an enzyme that belongs to the EROs family. ERO1L is expressed at high level in esophagus and upper digestive tract. ERO1L is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. ERO1L acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It associates with ERP44, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. ERO1L may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell. ERO1L responses to temperature stimulus, protein thiol-disulfide exchange, protein folding with or without chaperone cofactor and transport.
Research Area: Signal Transduction,