MABS1251
Anti-CYP11B2 Antibody, clone 41-17B
clone 41-17B, from mouse
Szinonimák:
Cytochrome P450 11B2, mitochondrial, CYP11B2, Aldosterone synthase, ALDOS, Aldosterone-synthesizing enzyme, CYPXIB2, Cytochrome P-450Aldo, Cytochrome P-450C18, Steroid 18-hydroxylase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(4)
About This Item
UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
antitest forma
purified immunoglobulin
antitest terméktípus
primary antibodies
klón
41-17B, monoclonal
faj reaktivitás
human
faj reaktivitás (homológia által előrejelzett)
mouse (based on 100% sequence homology)
technika/technikák
immunofluorescence: suitable
immunohistochemistry: suitable
western blot: suitable
izotípus
IgG1κ
NCBI elérési szám
UniProt elérési szám
kiszállítva
wet ice
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... CYP11B2(1585)
Általános leírás
Cytochrome P450 11B2, mitochondrial (EC1.14.15.4, EC1.14.15.5; UniProt P19099; also known as ALDOS, Aldosterone synthase, Aldosterone-synthesizing enzyme, CYPXIB2, Cytochrome P-450Aldo, Cytochrome P-450C18, Cytochrome P450 subfamily XIB polypeptide 2, Steroid 11-beta-monooxygenase, Steroid 11-beta/18-hydroxylase, Mitochondrial cytochrome P450 family 11 subfamily B polypeptide 2) is encoded by the CYP11B2 (Also known as CPN2, CYP11B, CYP11BL, P450C18) gene in human (Gene ID 1585). CYP11B2 protein is a member of the cytochrome P450 superfamily of monooxygenases that catalyze reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP11B2 protein is localized to the mitochondrial inner membrane and exhibits steroid 18-hydroxylase activity and steroid 11 beta-hydroxylase activity. CYP11B2 gene mutations are known causes of corticosterone methyl oxidase 1 (CMO-1) deficiency, an autosomal recessive disorder of aldosterone biosynthesis.
Immunogen
Chicken serum albumin-conjugated linear peptide corresponding to human CYP11B2 near the N-terminus.
Epitope: Near N-terminus
Alkalmazás
Anti-CYP11B2 Antibody, clone 41-17B is an antibody against CYP11B2 for use in Western Blotting, Immunohistochemistry, Immunofluorescence.
Immunohistochemistry Analysis: A representative lot detected CYP11B2 in normal adrenal glands (Gomez-Sanchez, C.E., et al. (2014). Mol. Cell Endocrinology. 383:111-117).
Immunofluorescence Analysis: A representative lot detected CYP11B2 in normal adrenal glands (Gomez-Sanchez, C.E., et al. (2014). Mol. Cell Endocrinology. 383:111-117).
Immunofluorescence Analysis: A representative lot detected CYP11B2 in normal adrenal glands (Gomez-Sanchez, C.E., et al. (2014). Mol. Cell Endocrinology. 383:111-117).
Research Category
Signaling
Signaling
Research Sub Category
Signaling Neuroscience
Signaling Neuroscience
Minőség
Evaluated by Western Blotting in hCYP11B2-GFP-expressing HEK293 cell lysate.
Western Blotting Analysis: 2.0 µg/mL of this antibody detected CYP11B2 in 10 µg of hCYP11B2-GFP-expressing HEK293 cell lysate.
Western Blotting Analysis: 2.0 µg/mL of this antibody detected CYP11B2 in 10 µg of hCYP11B2-GFP-expressing HEK293 cell lysate.
Cél megnevezése
~57 kDa observed
Fizikai forma
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Tárolás és stabilitás
Stable for 1 year at 2-8°C from date of receipt.
Egyéb megjegyzések
Concentration: Please refer to lot specific datasheet.
Jogi nyilatkozat
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Tárolási osztály kódja
12 - Non Combustible Liquids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Kazutaka Nanba et al.
The Journal of clinical endocrinology and metabolism, 103(10), 3869-3876 (2018-08-08)
Somatic mutations have been identified in more than half of aldosterone-producing adenomas (APAs) through mutation hotspot sequencing. The underlying pathogenesis of inappropriate aldosterone synthesis in the remaining population is still unknown. To investigate the prevalence and spectrum of somatic mutations
Wenjuan Liu et al.
Acta pharmaceutica Sinica. B, 12(1), 135-148 (2022-02-08)
Hyperaldosteronism is a common disease that is closely related to endocrine hypertension and other cardiovascular diseases. Cytochrome P450 11B2 (CYP11B2), an important enzyme in aldosterone (ALD) synthesis, is a promising target for the treatment of hyperaldosteronism. However, selective inhibitors targeting
Kei Omata et al.
Hypertension (Dallas, Tex. : 1979), 72(4), 874-880 (2018-10-26)
Primary aldosteronism affects ≈5% to 10% of hypertensive patients and has unilateral and bilateral forms. Most unilateral primary aldosteronism is caused by computed tomography-detectable aldosterone-producing adenomas, which express CYP11B2 (aldosterone synthase) and frequently harbor somatic mutations in aldosterone-regulating genes. The
Jimmy J Mao et al.
Journal of the Endocrine Society, 5(8), bvab107-bvab107 (2021-07-15)
The detection and management of concomitant pheochromocytoma (PHEO) and primary aldosteronism (PA) is not well understood. To investigate varying presentations and outcomes of cases with coexisting PHEO and PA to provide an approach to its diagnosis and management. We conducted
Chuanming Xu et al.
Acta physiologica (Oxford, England), 237(1), e13899-e13899 (2022-10-21)
The kaliuretic action of the renin-angiotensin-aldosterone system (RAAS) is well established as highlighted by hyperkalemia side effect of RAAS inhibitors but such action is usually ascribed to systemic RAAS. The present study addresses the involvement of intrarenal RAAS in K+
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