Recombinant Human Cytochrome P450 11B1, mitochondrial (CYP11B1)

Code CSB-EP006390HU
Size US$306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP006390HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CYP11B1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP006390HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CYP11B1.
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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
CYP11B1
Uniprot No.
Research Area
Cancer
Alternative Names
CYP11B1; S11BHCytochrome P450 11B1; mitochondrial; CYPXIB1; Cytochrome P-450c11; Cytochrome P450C11; Steroid 11-beta-hydroxylase; CYP11B1; EC 1.14.15.4
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
25-503aa
Target Protein Sequence
GTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
74.9 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

Customer Reviews and Q&A

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 Q&A
Q:

Please provide the following information regarding CSB-EP006390HU.
1.Sequence
2.Tag type
3.Tag position
4.Pricing, sizes and formats
Do you know if this product exhibits a P450 binding difference spectrum?

A:
Thanks for your inquiry.
Recombinant Human Cytochrome P450 11B1, mitochondrial(CYP11B1)
CSB-EP006390HU >> E.coli
You can view the full information of sequence and Tag on this page.
Sorry, as to whether this product exhibits a P450 binding difference spectrum, we haven't done any related research, we don't know about this.

Target Background

Function
A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids. Catalyzes the hydroxylation of carbon hydrogen bond at 11-beta position of 11-deoxycortisol and 11-deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or corticosterone, respectively. 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).
Gene References into Functions
  1. p.L340P CYP11B1 mutation is associated with 11beta-Hydroxylase deficiency. PMID: 29703198
  2. CYP11B1 silencing confirmed the lack of a significant metyrapone effect on mitotane action. The present findings do not support the view that CYP11B1 catalyzes a crucial step in the metabolic activation of mitotane and that CYP11B1 confers the adrenal specificity to mitotane PMID: 29734384
  3. we report clinical, genetic, hormonal, and structural effects of CYP11B1 gene mutations in the largest international cohort of 108 patients with steroid 11b-hydroxylase deficiency CAH. PMID: 28228528
  4. We conclude that 11 beta-OHD in Saudi Arabia has a unique genotype with a high rate of novel mutations. The novel p. R448P mutation is the most common mutation in this highly inbred population. PMID: 28962970
  5. One known and two novel CYP11B1 mutations are associated with congenital adrenal hyperplasia in a Chinese family. The two novel CYP11B1 mutations change heme binding site and decrease 11-hydroxylase activity in vitro. PMID: 28514642
  6. Data suggest that binding sites between CYP11B1/CYP11B2 and adrenodoxin/ferredoxin-1 exhibit electrostatic interactions at K370 in CYP11B1 and at K366 in CYP11B2 mutant R366K with D79 in adrenodoxin/ferredoxin-1. (CYP11B1 = cytochrome P450 family 11 subfamily B member 1; CYP11B2 = cytochrome P450 family 11 subfamily B member 2) PMID: 28355486
  7. analysis of CYP11B1 gene mutations in Turkish patients with 11-beta hydroxylase deficiency PMID: 26956189
  8. CYP11B1 mutants are a rare cause of congenital adrenal hyperplasia with hyperandrogenemia. PMID: 27376426
  9. Letter/Case Report: compound heterozygous CYP11B1 p.A199P/R448H mutation may predict severe congenital adrenal hypoplasia with severe hypokalemia leading to rhabdomyolysis. PMID: 27376433
  10. Data from a 19-year-old Chinese woman and her parents suggest congenital adrenal hyperplasia due to steroid 11beta-hydroxylase deficiency can be attributed to both a novel deletion mutation (g.9525_9526delCT, corresponding to p.L380V em leaderR420X) and a known missense mutation (g.5194G>C corresponding to p.D63H) in CYP11B1. [CASE-REPORT] PMID: 26806323
  11. Congenital adrenal hyperplasia caused by novel mutations in the CYP11B1 gene. PMID: 26476331
  12. Chimeric CYP11B2/CYP11B1 causing 11beta-hydroxylase deficiency in Chinese patients with congenital adrenal hyperplasia PMID: 26066897
  13. Seven novel CYP11B1 mutations identified in Chinese patients with 11 beta-hydroxylase deficiency. PMID: 25911436
  14. Mutations in the CYP11B1 gene are the cause of 11beta-hydroxylase deficiency. PMID: 25913739
  15. study of the functional consequences of 3 novel and 1 previously described CYP11B1 gene mutations (p.(Arg143Trp), p.(Ala306Val), p.(Glu310Lys) and p.(Arg332Gln)) detected in patients suffering from classical and non-classical 11beta-OHD PMID: 24022297
  16. Heterogenous immunolocalization of CYP11B2 and diffuse immunoreactivity of CYP11B1 were detected. PMID: 24837548
  17. Data from recombinant proteins suggest three additional mutations in CYP11B1 (p.His125Thrfs*8; p.Leu463_Leu464dup; p.Ser150Leu) can account for congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency (classical/non-classical phenotype). PMID: 24536089
  18. Analysis of the CYP11B1 gene revealed two novel mutations, a small insertion in exon 7 (InsAG393) and a small deletion in exon 2 (DelG766), and three previously known missense mutations (T318M, Q356X, and R427H). PMID: 23345044
  19. Expression of P45011beta and StAR (steroidogenic acute regulatory protein) is down-regulated in adrenocortical cells and neurons under oxidative stress by ALADIN (triple A syndrome protein, human) knockdown. PMID: 23825130
  20. Identification and functional characterization of a large deletion of the CYP11B1 gene causing an 11beta-Hydroxylase deficiency. PMID: 23146819
  21. Functional analysis of heterozygous human adrenal tissue demonstrated decreased CYP11B2 expression and increased CYP11B1 expression for those alleles associating with reduced risk of hypertension. PMID: 23150505
  22. CYP11B1 gene mutations were identified in nine patients, with a prevalent (p.R454C) and three novel mutations (p.V148G, IVS7-9C>A, c.1359_1360insG). PMID: 22964742
  23. Mutations in the CYP11B1 gene is associated with congenital adrenal hyperplasia. PMID: 22921894
  24. Hypertensives homozygous for the -344 T allele of CYP11B2 demonstrate altered 11beta-hydroxylase efficiency (CYP11B1); this is consistent with the hypothesis of a genetically determined increase in adrenal ACTH drive in these subjects. PMID: 17651452
  25. Both CMO I/CYP11B1 and CMO II/CYP11B2 (expressed as recombinant proteins in COS-7 cells) exhibit steroid 11-beta-hydroxylase activity, but only CMO II/CYP11B2 exhibits steroid 18-hydroxylase activity to form aldosterone. [REVIEW] PMID: 22217843
  26. We describe a family with an atypical CYP11B1/CYP11B2 gene inheritance pattern and variable phenotypic expression, where the majority of pediatric patients have primary aldosteronism. PMID: 22083159
  27. CYP11B1 is overexpressed in subclinical cortisol-producing adenomas and its overexpression accounts for the increased production of cortisol PMID: 21848792
  28. a definitive diagnosis of glucocorticoid-remediable aldosteronism can only be obtained by identification of the CYP11B1/CYP11B2 chimeric gene PMID: 21625068
  29. Results describe an unprecedented case of unequal cross-over mutation for the chimeric CYP11B1/CYP11B2 gene causing familial hyperaldosteronism-I, which may be linked to a polymorphism in the index case's father germ line. PMID: 20634641
  30. A novel missense mutation (p.R454C) in the CYP11B1 gene was identified PMID: 20947076
  31. Importance of adrenal steroid synthesis in the development of hypertension and cardiovascular dysfunction as well as the role of common polymorphisms in adrenal synthetic genes in altering corticosteroid biosynthesis. PMID: 21164264
  32. in 15 unrelated Tunisian patients with classical 11beta-hydroxylase deficiency, only 2 mutations were detected in homozygous state in the CYP11B1 gene, the p.Q356X in exon 6 (26.6%) and the novel p.G379V in exon 7 with large prevalence (73.3%) PMID: 20331679
  33. Each CYP11B1 mutation is new and private, contrasting with the high incidence of two Tunisian mutations. PMID: 20523022
  34. The chimeric gene CYP11B1/CYP11B2 (crossover to be located between intron 2 of CYP11B1 and exon 3 of CYP11B2) cause Glucocorticoid-remediable aldosteronism. (CTP11B1) PMID: 20808686
  35. Aldosterone-producing adenoma patients were genotyped for rs6410 (G22 5A)& rs6387 (A2803G). DNA polymorphisms at CYP11B2/B1 locus may confer susceptibility to postoperative hypertension of patients with APA. PMID: 20708777
  36. there was a significant association between polymorphisms in the CYP11B2 and CYP11B1 genes and a genetic predisposition to idiopathic hyperaldosteronism. PMID: 20339375
  37. Functional analysis results allow for the classification of novel CYP11B1 mutations as causative for classic and nonclassic 11OHD, respectively. PMID: 20089618
  38. role in familial hyperaldosteronism PMID: 11903322
  39. Differential regulation of aldosterone synthase and 11beta-hydroxylase transcription by steroidogenic factor-1 PMID: 11932209
  40. novel nonsense mutation that converts codon 265 CAG (glutamine) to TAG (stop) of exon 4; patient suffers from complete loss of the final step in cortisol biosynthesis pathway because of the nonsense mutation PMID: 14682466
  41. Molecular variant in CYP11B2 is in linkage disequilibrium (LD) with a key quantitative trait in CYP11B1. PMID: 15507509
  42. Linkage disequilibrium between causative CYP11B1 variants and CYP11B2 polymorphisms account for urinary 11-deoxycortisol excretion. PMID: 15522937
  43. Mutations are associated with congenital adrenal hyperplasia. PMID: 15699546
  44. DNA analysis of the gene (CYP11B1) encoding 11beta-hydroxylase was used in the prenatal diagnosis of 11beta-hydroxylase deficiency, and prenatal dexamethasone treatment was successful in preventing virilization in one affected female fetus. PMID: 15751602
  45. L299P mutation causes a change in the position of the I helix relative to the heme group, whereas the DeltaF438 mutation results in a steric disarrangement of the heme group relative to the enzyme giving rise sto congenital adrenal hyperplasia. PMID: 15755848
  46. Micro-satellite polymorphism (tttta)n of gene CYP11 alpha exists in Chinese women and the polymorphism does not relate to the pathogenesis of hyperandrogenism in women with polycystic ovary syndrome. PMID: 15793791
  47. PCB126 up-regulates steroidogenic CYP11B1 and CYP11B2 mRNA expression not via AhR-mediated transcriptional activation but by increasing posttranscriptional mRNA stability PMID: 16396990
  48. Aldosterone synthesis is highly heritable and is affected by genotype at CYP11B1. PMID: 16984984
  49. Impaired 11beta-hydroxylase efficiency associated previously with the CYP11B2 -344 and intron conversion variants is because of linkage with these newly identified polymorphisms in CYP11B1. PMID: 17075029
  50. no variants were identified in the coding region of CYP11B1 that could account for hypertension and/or a raised aldosterone to renin ratio; however study identifies the importance of these affected residues to enzyme function PMID: 17121536

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Involvement in disease
Adrenal hyperplasia 4 (AH4); Hyperaldosteronism, familial, 1 (HALD1)
Subcellular Location
Mitochondrion inner membrane; Peripheral membrane protein.
Protein Families
Cytochrome P450 family
Database Links

HGNC: 2591

OMIM: 103900

KEGG: hsa:1584

STRING: 9606.ENSP00000292427

UniGene: Hs.184927

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