

| Catalog No. | HD122012 |
|---|---|
| Description |
Recombinant Human CYP4F2 Protein, N-His (HD122012) expressed in E. coli, spanning Gly62-Ser520. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | P78329 |
| Protein length | Gly62-Ser520 |
| 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 | 54.89 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, Arachidonic acid omega-hydroxylase, CYP4F2, CYPIVF2, Cytochrome P450 4F2, Cytochrome P450-LTB-omega, Docosahexaenoic acid omega-hydroxylase, EC:1.14.14.1, EC:1.14.14.78, EC:1.14.14.79, EC:1.14.14.94, Leukotriene-B(4) 20-monooxygenase 1, Leukotriene-B(4) omega-hydroxylase 1, Phylloquinone omega-hydroxylase CYP4F2 |
| Background | Cytochrome P450 4F2 is a ~59 kDa protein. A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins. 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 long- and very long-chain fatty acids. Displays high omega-hydroxylase activity toward polyunsaturated fatty acids (PUFAs). Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. 1. Lasker, JM. et al. (2000) The Journal of biological chemistry 275, 4118-26. PMID: 10660572 2. Kikuta, Y. et al. (2000) Journal of biochemistry 127, 1047-52. PMID: 10833273 3. Sontag, TJ. et al. (2002) The Journal of biological chemistry 277, 25290-6. PMID: 11997390 4. Stec, DE. et al. (2007) Physiological genomics 30, 74-81. PMID: 17341693 5. Fava, C. et al. (2008) Hypertension (Dallas, Tex. : 1979) 52, 373-80. PMID: 18574070 6. Fer, M. et al. (2008) Journal of lipid research 49, 2379-89. PMID: 18577768 |
| Note | For research use only |
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