

| Catalog No. | HD012012 |
|---|---|
| Description |
Recombinant Human CYP11B2 Protein, N-His (HD012012) expressed in E. coli, spanning Gly25-Asn503. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | P19099 |
| Protein length | Gly25-Asn503 |
| 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 | 57.25 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 | ALDOS, Aldosterone synthase, Aldosterone-synthesizing enzyme, CYP11B2, CYPXIB2, Corticosterone 18-monooxygenase, CYP11B2, Cytochrome P-450Aldo, Cytochrome P-450C18, Cytochrome P450 11B2, mitochondrial, EC:1.14.15.4, EC:1.14.15.5, Steroid 11-beta-hydroxylase, CYP11B2, Steroid 18-hydroxylase |
| Background | Cytochrome P450 11B2, mitochondrial is a ~57 kDa protein. A cytochrome P450 monooxygenase that catalyzes the biosynthesis of aldosterone, the main mineralocorticoid in the human body responsible for salt and water homeostasis, thus involved in blood pressure regulation, arterial hypertension, and the development of heart failure. Catalyzes three sequential oxidative reactions of 11-deoxycorticosterone (21-hydroxyprogesterone), namely 11-beta hydroxylation, followed by two successive oxidations at C18 yielding 18-hydroxy and then 18-oxo intermediates (that would not leave the enzyme active site during the consecutive hydroxylation reactions), ending with the formation of aldosterone. Can also produce 18-hydroxycortisol and 18-oxocortisol, derived from successive oxidations of cortisol at C18, normally found at very low levels, but significantly increased in primary aldosteronism, the most common form of secondary hypertension. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin). 1. Bechtel, S. et al. (2002) European journal of biochemistry 269, 1118-27. PMID: 11856349 2. Bureik, M. et al. (2002) Endocrine research 28, 351-5. PMID: 12530636 3. Pascoe, L. et al. (1992) Proceedings of the National Academy of Sciences of the United States of America 89, 8327-31. PMID: 1518866 4. Freel, EM. et al. (2004) The Journal of clinical endocrinology and metabolism 89, 4628-33. PMID: 15356073 5. Pascoe, L. et al. (1992) Proceedings of the National Academy of Sciences of the United States of America 89, 4996-5000. PMID: 1594605 6. Curnow, KM. et al. (1991) Molecular endocrinology (Baltimore, Md.) 5, 1513-22. PMID: 1775135 7. Hobler, A. et al. (2012) The Journal of steroid biochemistry and molecular biology 132, 57-65. PMID: 22446688 8. Strushkevich, N. et al. (2013) Molecular endocrinology (Baltimore, Md.) 27, 315-24. PMID: 23322723 9. Mulatero, P. et al. (1998) The Journal of clinical endocrinology and metabolism 83, 3996-4001. PMID: 9814482 10. Portrat-Doyen, S. et al. (1998) The Journal of clinical endocrinology and metabolism 83, 4156-61. PMID: 9814506 |
| Note | For research use only |
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