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HSD11B2 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P80365 |
|---|
| Gene ID | 3291 |
|---|---|
| Other Names | Corticosteroid 11-beta-dehydrogenase isozyme 2, 111-, 11-beta-hydroxysteroid dehydrogenase type 2, 11-DH2, 11-beta-HSD2, 11-beta-hydroxysteroid dehydrogenase type II, -HSD11 type II, NAD-dependent 11-beta-hydroxysteroid dehydrogenase, 11-beta-HSD, HSD11B2, HSD11K |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | HSD11B2 (HGNC:5209) |
|---|---|
| Function | Catalyzes the conversion of biologically active 11beta- hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) (PubMed:7859916, PubMed:8538347, PubMed:10497248, PubMed:22796344, PubMed:27927697, PubMed:30902677, PubMed:33387577, PubMed:12788846, PubMed:17314322). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids (PubMed:7859916, PubMed:10497248, PubMed:33387577, PubMed:12788846, PubMed:17314322). Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen (PubMed:22796344, PubMed:27927697). Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost- 4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17- trione), which can be further metabolized to 11-ketotestosterone (PubMed:27927697). Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25- hydroxycholesterol in vitro (PubMed:30902677). 7-beta-25- dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as a ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (PubMed:30902677). May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (By similarity). |
| Cellular Location | Microsome. Endoplasmic reticulum |
| Tissue Location | Expressed in kidney, placenta, pancreas, prostate, ovary, small intestine and colon, and in lower levels in the spleen and testis (PubMed:7859916). At midgestation, expressed at high levels in placenta and in fetal kidney and, at much lower levels, in fetal lung and testis (PubMed:8530071). |
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Provided below are standard protocols that you may find useful for product applications.
Background
There are at least two isozymes of the corticosteroid 11-beta-dehydrogenase, a microsomal enzyme complex responsible for the interconversion of cortisol and cortisone. The type I isozyme has both 11-beta-dehydrogenase (cortisol to cortisone) and 11-oxoreductase (cortisone to cortisol) activities. The type II isozyme, encoded by this gene, has only 11-beta-dehydrogenase activity. In aldosterone-selective epithelial tissues such as the kidney, the type II isozyme catalyzes the glucocorticoid cortisol to the inactive metabolite cortisone, thus preventing illicit activation of the mineralocorticoid receptor. In tissues that do not express the mineralocorticoid receptor, such as the placenta and testis, it protects cells from the growth-inhibiting and/or pro-apoptotic effects of cortisol, particularly during embryonic development. Mutations in this gene cause the syndrome of apparent mineralocorticoid excess and hypertension.
References
Li, J., et al. Breast Cancer Res. 12 (2), R19 (2010) Ni, X.T., et al. Placenta 30(12):1023-1028(2009)Mericq, V., et al. Eur. J. Endocrinol. 161(3):419-425(2009)Stark, M.J., et al. Am. J. Physiol. Regul. Integr. Comp. Physiol. 297 (2), R510-R514 (2009) Lepenies, J., et al. Clin. Exp. Hypertens. 31(4):376-379(2009)
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