Recombinant Human Cytochrome P450 11B1, Mitochondrial (CYP11B1) Protein (His-SUMO&Myc)

Name: Recombinant Human Cytochrome P450 11B1, Mitochondrial (CYP11B1) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-09285P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CYP11B1.

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Product Overview

Description	Recombinant Human Cytochrome P450 11B1, Mitochondrial (CYP11B1) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P15538
Target Symbol	CYP11B1
Synonyms	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)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	GTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN
Expression Range	25-503aa
Protein Length	Full Length of Mature Protein
Mol. Weight	74.9 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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).
Subcellular Location	Mitochondrion inner membrane; Peripheral membrane protein.
Protein Families	Cytochrome P450 family
Database References	HGNC: 2591 OMIM: 103900 KEGG: hsa:1584 STRING: 9606.ENSP00000292427 UniGene: Hs.184927
Associated Diseases	Adrenal hyperplasia 4 (AH4); Hyperaldosteronism, familial, 1 (HALD1)

Gene Functions References

p.L340P CYP11B1 mutation is associated with 11beta-Hydroxylase deficiency. PMID: 29703198
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
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
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
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
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
analysis of CYP11B1 gene mutations in Turkish patients with 11-beta hydroxylase deficiency PMID: 26956189
CYP11B1 mutants are a rare cause of congenital adrenal hyperplasia with hyperandrogenemia. PMID: 27376426
Letter/Case Report: compound heterozygous CYP11B1 p.A199P/R448H mutation may predict severe congenital adrenal hypoplasia with severe hypokalemia leading to rhabdomyolysis. PMID: 27376433
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
Congenital adrenal hyperplasia caused by novel mutations in the CYP11B1 gene. PMID: 26476331
Chimeric CYP11B2/CYP11B1 causing 11beta-hydroxylase deficiency in Chinese patients with congenital adrenal hyperplasia PMID: 26066897
Seven novel CYP11B1 mutations identified in Chinese patients with 11 beta-hydroxylase deficiency. PMID: 25911436
Mutations in the CYP11B1 gene are the cause of 11beta-hydroxylase deficiency. PMID: 25913739
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
Heterogenous immunolocalization of CYP11B2 and diffuse immunoreactivity of CYP11B1 were detected. PMID: 24837548
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
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
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
Identification and functional characterization of a large deletion of the CYP11B1 gene causing an 11beta-Hydroxylase deficiency. PMID: 23146819
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
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
Mutations in the CYP11B1 gene is associated with congenital adrenal hyperplasia. PMID: 22921894
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
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
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
CYP11B1 is overexpressed in subclinical cortisol-producing adenomas and its overexpression accounts for the increased production of cortisol PMID: 21848792
a definitive diagnosis of glucocorticoid-remediable aldosteronism can only be obtained by identification of the CYP11B1/CYP11B2 chimeric gene PMID: 21625068
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
A novel missense mutation (p.R454C) in the CYP11B1 gene was identified PMID: 20947076
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
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
Each CYP11B1 mutation is new and private, contrasting with the high incidence of two Tunisian mutations. PMID: 20523022
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
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
there was a significant association between polymorphisms in the CYP11B2 and CYP11B1 genes and a genetic predisposition to idiopathic hyperaldosteronism. PMID: 20339375
Functional analysis results allow for the classification of novel CYP11B1 mutations as causative for classic and nonclassic 11OHD, respectively. PMID: 20089618
role in familial hyperaldosteronism PMID: 11903322
Differential regulation of aldosterone synthase and 11beta-hydroxylase transcription by steroidogenic factor-1 PMID: 11932209
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
Molecular variant in CYP11B2 is in linkage disequilibrium (LD) with a key quantitative trait in CYP11B1. PMID: 15507509
Linkage disequilibrium between causative CYP11B1 variants and CYP11B2 polymorphisms account for urinary 11-deoxycortisol excretion. PMID: 15522937
Mutations are associated with congenital adrenal hyperplasia. PMID: 15699546
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
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
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
PCB126 up-regulates steroidogenic CYP11B1 and CYP11B2 mRNA expression not via AhR-mediated transcriptional activation but by increasing posttranscriptional mRNA stability PMID: 16396990
Aldosterone synthesis is highly heritable and is affected by genotype at CYP11B1. PMID: 16984984
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
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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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