Specification
| Description | Recombinant protein from the full-length sequence of Homo sapiens cytochrome P450 family 2 subfamily W member 1 (CYP2W1) (NM_017781). |
| Organism | Homo sapiens (Human) |
| Expression Host | Human Cells |
| Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
| Purity | Greater than 90% by SDS-PAGE gel |
| Uniprot ID | Q8TAV3 |
| Entry Name | CP2W1_HUMAN |
| Gene Names | CYP2W1 |
| Alternative Gene Names | |
| Alternative Protein Names | Cytochrome P450 2W1 (EC 1.14.14.-) (CYPIIW1) |
| Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
| Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
| Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
| Length | 490 |
| Molecular Weight(Da) | 53844 |
| Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MALLLLLFLGLLGLWGLLCACAQDPSPAARWPPGPRPLPLVGNLHLLRLSQQDRSLMELSERYGPVFTVHLGRQKTVVLTGFEAVKEALAGPGQELADRPPIAIFQLIQRGGGIFFSSGARWRAARQFTVRALHSLGVGREPVADKILQELKCLSGQLDGYRGRPFPLALLGWAPSNITFALLFGRRFDYRDPVFVSLLGLIDEVMVLLGSPGLQLFNVYPWLGALLQLHRPVLRKIEEVRAILRTLLEARRPHVCPGDPVCSYVDALIQQGQGDDPEGLFAEANAVACTLDMVMAGTETTSATLQWAALLMGRHPDVQGRVQEELDRVLGPGRTPRLEDQQALPYTSAVLHEVQRFITLLPHVPRCTAADTQLGGFLLPKGTPVIPLLTSVLLDETQWQTPGQFNPGHFLDANGHFVKREAFLPFSAGRRVCVGERLARTELFLLFAGLLQRYRLLPPPGVSPASLDTTPARAFTMRPRAQALCAVPRP |
Background
| Function | FUNCTION: A cytochrome P450 monooxygenase that may play a role in retinoid and phospholipid metabolism (PubMed:22591743, PubMed:26936974). Catalyzes the hydroxylation of saturated carbon hydrogen bonds. Hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may regulate atRA clearance. Other retinoids such as all-trans retinol and all-trans retinal are potential endogenous substrates (PubMed:26936974). Catalyzes both epoxidation of double bonds and hydroxylation of carbon hydrogen bonds of the fatty acyl chain of 1-acylphospholipids/2-lysophospholipids. Can metabolize various lysophospholipids classes including lysophosphatidylcholines (LPCs), lysophosphatidylinositols (LPIs), lysophosphatidylserines (LPSs), lysophosphatidylglycerols (LPGs), lysophosphatidylethanolamines (LPEs) and lysophosphatidic acids (LPAs) (PubMed:22591743). Has low or no activity toward 2-acylphospholipids/1-lysophospholipids, diacylphospholipids and free fatty acids (PubMed:26936974, PubMed:22591743). May play a role in tumorigenesis by activating procarcinogens such as aflatoxin B1, polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines (PubMed:20805301, PubMed:16551781, PubMed:24278521). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:22591743, PubMed:26936974). {ECO:0000269|PubMed:16551781, ECO:0000269|PubMed:20805301, ECO:0000269|PubMed:22591743, ECO:0000269|PubMed:24278521, ECO:0000269|PubMed:26936974}. |
| Pathway | |
| Protein Families | Cytochrome P450 family |
| Tissue Specificity | Very low levels are detected in fetal and adult tissues. Highly expressed in several tumor samples, in particular colon and adrenal tumors. {ECO:0000269|PubMed:16426568}. |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |