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We validate the specificity of these antibodies to CYP11A1 by testing them on tissues known to express CYP11A1 positively and negatively. Browse below to find the CYP11A1 antibody that suites your experiment. We have 6 of these antibodies and many publications and validation images.
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Facts about Cholesterol side-chain cleavage enzyme, mitochondrial.
|cytochrome P450 family|
Cholesterol desmolase; cholesterol monooxygenase (side-chain-cleaving); cholesterol side-chain cleavage enzyme, mitochondrial; CYPXIA1; Cytochrome P450 11A1; Cytochrome P450(scc); cytochrome P450, family 11, subfamily A, polypeptide 1; cytochrome P450C11A1; EC 1.14.15; EC 18.104.22.168; steroid 20-22-lyase; subfamily XIA (cholesterol side chain cleavage)
|Sequence:||15; NC_000015.10 (74337762..74367646, complement)|
Mitochondrion inner membrane; Peripheral membrane protein. Localizes to the matrix side of the mitochondrion inner membrane.
The enzyme CYP11A1 is responsible for the metabolism of vitamin D3. This enzyme also regulates the rate-limiting phase in the process of steroidogenesis. This enzyme is an essential component of the human metabolism system and is utilized to detect substances that cause disease. It regulates cholesterol's access to CYP11A1.
The CYP11A1 enzyme is responsible for the metabolism of vitamin (D)3. The hydroxylation (hydroxylation) of vitamin D3 has revealed the existence of a brand new metabolite. It has a high biological potencyand it has a C20 structural structure, and specific effects depending upon the cell lineage. It does not have toxic effects at high doses of pharmacological dosage.
The metabolites of vitamin D3 are created by the reconstituting CYP11A1 enzyme. The hydroxyl group at the C20 position is an epi-like structure which suggests that vitamin D3 metabolisms could serve biological functions. However, the metabolites are yet to be determined. They could have bioactive properties that are unique to them , and will be very valuable in the near future.
This enzyme has been known to metabolize cholesterol and 7-dehydrocholesterol. It has been shown to be capable of metabolizing cholesterol and 7-dehydrocholesterol. This could be a theoretical basis for supplementing vitamin D3 during pregnancy.
Overexpression of CYP11A1 can cause negative effects on BeWo cells and NSCs and other tissues. NSCs cultured in BeWo condition medium showed lower growth and DNA damage. However, vitamin D3-treated NSCs had lower rates of lesion formation. In the field of cancer research it may be advantageous to investigate the role of CYP11A1 as well as vitamin D3 metabolism.
The CYP11A1 enzyme also triggers the metabolism of vitamin D3 in the body. UVB radiation also activates the secosteroidogenic pathway. It is a paradigm shift in both biology and medicine. It is low in toxicity and has a variety of functional phenotypes. It has been discovered that this enzyme catalyzes the metabolism of vitamin D3 in the liver.
The CYP11A1 homolog of HPA is known to be expressed in the skin dermis and epidermis. Expression of CYP11A1 is induced in cells by UVB exposure. Furthermore, UVB-induced expression of CYP11A1 may be accompanied by an increase in the expression of HPA axis elements. CYP11A1 expression is also controlled by UVR, which is extremely powerful. It could function through an HPA-like system. Locally manufactured ACTH or CRF may also be utilized as messengers.
The growth of melanocytes derived from CYP11A1 as well as of growth in soft agar are both caused by secosteroids. Additionally, 20(OH)D3 inhibits TNFa and IL-6 production, thereby suppressing the production of proinflammatory chemicals and stimulating the production of the anti-inflammatory cytokine, I-10 in humans. The biosynthesis of vitamin D3 is dependent on the CYP11A1 enzyme.
CYP11A1 upregulation in the fetal mind could influence fetal neurodevelopment. Similar to this, the overexpression of the CYP11A1 gene in the placenta may also cause adverse effects on the brain of the fetus, including cognitive dysfunction. Therefore, the upregulation of CYP11A1 in fetal brain is necessary to study the effects of bisphenol A on the development of neurons.
Steroid hormones play a crucial role in the regulation of several physiological processes, including salt balance and glucose. They are linked with illnesses when they aren't properly released. In humans, CYP11A1 regulates the first step in steroid biosynthesis. This enzyme is located in the adrenal cortex and the gonads. It is controlled by pituitary hormones and as well as the signaling pathway cAMP. The enzyme is also involved in tissue-specific expression of steroids-related genes.
The genome CYP11A1 encodes an enzyme called the cytochrome P450side-chain cleavage which is vital for the production of steroids. Previous studies on zebrafish revealed that cyp11a2 functions as the equivalent of human CYP11A1 interrenal Steroidogenesis. However, the function of Cyp11a2 in adult zebrafish is in the dark.
The first step in steroidogenesis involves the conversion of cholesterol into pregnenolone. This process is made easier by the P450scc which is located within mitochondria. The oxidative enzymes transform pregnenolone to the other steroids. However the conversion of cholesterol to pregnenolone is a crucial regulatory step.
Another step in the steroidogenesis pathway is the conversion of CD8+ cells from IFN g-mediated to IL-13-producing T cells. This is crucial for lung allergic reactions, as it links steroidogenesis and proallergic differentiation pathways. It isn't fully known despite its essential role within the immune system.
In addition, the molecular underlying of the immune-modulatory effect of steroids remains largely unknown. Studies have proven that local extra-glandular steroids play a role in the regulation of inflammation and immunity. Unanswered questions may result in an exciting new era of study of steroid hormones in future.
One study found that 46-XY sufferers had a CYP11A1 defect. The patient was born prematurely with sex reversed, and suffered severe adrenal insufficiency. Tests revealed that the CYP11A1 gene contained the mutation that eliminated an adenine in exon position 835. The mutation was expected to delete the P450scc region that is conserved by the enzyme. However, the authors emphasized that this was the first case of a mutation that causes disruption in an acquired gene.
The study also revealed that noncoding RNAs showed little or no relationship to the steroid metabolism. However it is possible to apply metabolic flux analysis to study this intricate process in immune cells. Multimodal omics and single-cell transcriptome-genome analyses are two of the most modern techniques that can be utilized to study the complex biosynthesis of steroid pathways in immune cells.
Previous studies have shown that CYP11A1 may be associated with androgen-related phenotypes. However previous studies overestimated the association. Additionally, CYP11A1 has been shown to be essential in the conversion of CD8+ T cells into IL-13-producing cells. Cyp11A1 inhibitors stop this conversion and inhibit steroidogenesis.
The metabolism of cholesterol is controlled by the cytochrome P450 enzyme CYP11A1. This enzyme cuts side chains of cholesterol and releases its active constituents. It is present in the primary osteoblasts as well as human bone tissue. However, there is not much information about its role in the regulation of cholesterol metabolism.
The sequence of CYP11A1 differs between humans and closely related mammalian species. The rat and human the CYP11A1s possess more than ninety percent identity, but the differences between the two enzymes are quite striking. Both human and rat CYP11A1 exhibit similar Km values in conjunction with cholesterol, however, the human enzyme shows lower Kcat/Km values than its bovine counterpart.
In mice, the enzymatic activity of CYP11A1 is induced by the sensitization of peanuts and the challenge. AMG was able to block Cyp11a1 activity but not its expression of its protein. The Cyp11a1 inhibitor was administered by gavage to the mice. The immunohistochemical staining was used to determine Cyp11a1 levels in the jejunum.
The CYP11A1 enzyme is found in the liver and kidneys. It converts cholesterol, desmosterol, and plant sterols, to the hormone pregnenolone. The enzyme prefers 7-dehydrocholesterol (7DHC) as its primary substrate, whereas vitamin D3 and D2 are not good substrates. These conversions may also be carried out in the epidermis and adrenal glands as well in serum.
The CYP11A1 gene is located on chromosome 15. It was first identified in human spermatozoa and mice, via Southern analysis of a panel mouse-human somatic cell hybrid. A subsequent study by Youngblood and Sparkes and Sparkes. revealed a close connection between CYP11A and CYP19 homologs. This gene is located at 15q21.1.
The expression of CYP11A1 in human cells is regulated by physical and diet. Cyp11a1 plays an important role in the regulation of TH2 cell differentiation and the production cytokines. CYP11A1 regulates cholesterol upregulation and the access to fatty acids through the hepatic sphingosamin.
The link between the CYP11A1 gene with PCOS is mostly indirect, however, there is some evidence that the gene plays a role. There are a variety of polymorphisms within the CYP11A1 gene that have been associated with various hormone-related disorders. One of these polymorphisms was associated with PCOS. The polymorphism in the CYP11A1 gene was also found to be associated with the results of a study that involved South Indian women.
*More publications can be found for each product on its corresponding product page