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CYP51A1 encodes a member of the cytochrome P450 superfamily of enzymes. Additionally we are shipping Cytochrome P450, Family 51, Subfamily A, Polypeptide 1 Proteins (4) and and many more products for this protein.
Showing 10 out of 75 products:
Human Polyclonal CYP51A1 Primary Antibody for ELISA, WB - ABIN560552
Watanabe, Hirai, Tateno, Fukui: Variation of cholesterol contents in porcine cumulus-oocyte complexes is a key factor in regulation of fertilizing capacity. in Theriogenology 2013
Show all 2 Pubmed References
the regulation of expression of human CYP51A1, the lanosterol 14alpha-demethylase, is reported.
Molecular insights regarding substrate profile, faster catalysis, and weaker susceptibility of human CYP51 to inhibition.
Acyl-Carbon Bond Cleaving Cytochrome P450 Enzymes: CYP17A1, CYP19A1 and CYP51A1.
Suggest that GDF9, possibly with FSH, may play significant roles in the regulation of cholesterol biosynthesis and the expression of CYP51A1 in granulosa cells which might be a predictor for unfertilization.
Data show that forkhead transcription factor 4 (FoxO4) interacts with sterol regulatory element binding protein (SREBP)2 and hypoxia inducible factor (HIF)2alpha to modulate lanosterol 14alpha demethylase (CYP51) promoter activity.
Our results indicate a new link between a cholesterol synthesis gene CYP51A1 and pregnancy pathologies.
The studied azoles selectively interacted with human cytochrome P450 51A1, which showed the highest affinity towards ketoconazole.
Low nucleotide variability of CYP51A1 is seen in cholesterol and bile acid synthesis and xenobiotic metabolism pathways.
The new CYP51A1 inhibitor 2-((3,4-dichlorophenethyl)(propyl)amino)-1-(pyridin-3-yl)ethanol (LEK-935) on the proteome of primary human hepatocytes were analyzed.
Studies indicate that CPY51 structures from various eukaryotic organisms are strikingly similar.
The substantial conformational changes in the B' helix and F-G loop regions are induced upon ligand binding, consistent with the membrane nature of the protein and its substrate.
A cAMP-responsive element binding site is essential for sterol regulation of the human lanosterol 14alpha-demethylase gene.
Plays primary roles in determining strength of interactions with azoles
the liver X receptor alpha directly silencing the expression of two key cholesterologenic enzymes (lanosterol 14alpha-demethylase (CYP51A1), and squalene synthase (farnesyl diphosphate farnesyl transferase 1)) via novel negative LXR DNA response elements
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This endoplasmic reticulum protein participates in the synthesis of cholesterol by catalyzing the removal of the 14alpha-methyl group from lanosterol. Homologous genes are found in all three eukaryotic phyla, fungi, plants, and animals, suggesting that this is one of the oldest cytochrome P450 genes. Two transcript variants encoding different isoforms have been found for this gene.
, cytochrome P450 51A1
, cytochrome P450, 51 (lanosterol 14-alpha-demethylase)
, cytochrome P450-14DM
, cytochrome P45014DM
, cytochrome P450LI
, lanosterol 14-alpha demethylase
, lanosterol 14-alpha-demethylase
, sterol 14-alpha demethylase
, Cytochrome P450 51A1
, lanosterol 14-demethylase
, cytochrome P450, family 51, subfamily A, polypeptide 1