

| Catalog No. | HC231012 |
|---|---|
| Description |
Recombinant Human CYP4A11 Protein, N-His (HC231012) expressed in E. coli, spanning Met1-Leu519. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | Q02928 |
| Protein length | Met1-Leu519 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 61.51 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | 20-HETE synthase, 20-hydroxyeicosatetraenoic acid synthase, CYP4A11, CYP4A2, CYP4AII, CYPIVA11, Cytochrome P-450HK-omega, Cytochrome P450 4A11, Cytochrome P450HL-omega, EC:1.14.14.1, EC:1.14.14.80, Fatty acid omega-hydroxylase, Lauric acid omega-hydroxylase, Long-chain fatty acid omega-monooxygenase |
| Background | Cytochrome P450 4A11 is a ~59 kDa protein. A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins). 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). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)-octadecadienoic > hexadecanoic acid. Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver. Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. 1. Adas, F. et al. (1999) Journal of lipid research 40, 1990-7. PMID: 10553002 2. Lasker, JM. et al. (2000) The Journal of biological chemistry 275, 4118-26. PMID: 10660572 3. Gainer, JV. et al. (2005) Circulation 111, 63-9. PMID: 15611369 4. Kawashima, H. et al. (1992) Biochimica et biophysica acta 1123, 156-62. PMID: 1739747 5. Palmer, CN. et al. (1993) Biochimica et biophysica acta 1172, 161-6. PMID: 7679927 6. Powell, PK. et al. (1996) Archives of biochemistry and biophysics 335, 219-26. PMID: 8914854 8. Sanders, RJ. et al. (2008) FASEB journal : official publication of the Federation of American Societies for Experimental Biology 22, 2064-71. PMID: 18182499 |
| Note | For research use only |
Contact us for custom quotes, bulk requests and any other issues.
Mail: [email protected]
+86-27-65523339
Building C, No. 666, Shen Dun Si Lu, Wuhan, 430206, China
中文
English
한국어
日本語
Español
Français
Русский